{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,9]],"date-time":"2026-06-09T07:04:38Z","timestamp":1780988678711,"version":"3.54.1"},"reference-count":198,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/100010874","name":"American Society for Bone and Mineral Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100010874","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["DK116716"],"award-info":[{"award-number":["DK116716"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["DK011794"],"award-info":[{"award-number":["DK011794"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bone"],"published-print":{"date-parts":[[2021,2]]},"DOI":"10.1016\/j.bone.2020.115606","type":"journal-article","created":{"date-parts":[[2020,8,20]],"date-time":"2020-08-20T12:34:50Z","timestamp":1597926890000},"page":"115606","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":15,"special_numbering":"C","title":["Role of histone deacetylases in bone development and skeletal disorders"],"prefix":"10.1016","volume":"143","author":[{"given":"Jialiang S.","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sung-Hee","family":"Yoon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marc N.","family":"Wein","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"7766","key":"10.1016\/j.bone.2020.115606_bb0005","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1038\/s41586-019-1411-0","article-title":"Advances in epigenetics link genetics to the environment and disease","volume":"571","author":"Cavalli","year":"2019","journal-title":"Nature"},{"issue":"4139","key":"10.1016\/j.bone.2020.115606_bb0010","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1126\/science.184.4139.865","article-title":"Chromatin structure; oligomers of the histones","volume":"184","author":"Kornberg","year":"1974","journal-title":"Science"},{"issue":"6648","key":"10.1016\/j.bone.2020.115606_bb0015","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1038\/38444","article-title":"Crystal structure of the nucleosome core particle at 2.8 A resolution","volume":"389","author":"Luger","year":"1997","journal-title":"Nature"},{"issue":"4","key":"10.1016\/j.bone.2020.115606_bb0020","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/j.cell.2007.02.005","article-title":"Chromatin modifications and their function","volume":"128","author":"Kouzarides","year":"2007","journal-title":"Cell"},{"issue":"1","key":"10.1016\/j.bone.2020.115606_bb0025","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1038\/nrg2905","article-title":"Charting histone modifications and the functional organization of mammalian genomes","volume":"12","author":"Zhou","year":"2011","journal-title":"Nat Rev Genet"},{"issue":"4","key":"10.1016\/j.bone.2020.115606_bb0030","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1038\/nrm2145","article-title":"Histone acetyltransferase complexes: one size doesn't fit all","volume":"8","author":"Lee","year":"2007","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"1","key":"10.1016\/j.bone.2020.115606_bb0035","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/0006-291X(69)90661-5","article-title":"Enzymatic deacetylation of histone","volume":"36","author":"Inoue","year":"1969","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"4","key":"10.1016\/j.bone.2020.115606_bb0040","doi-asserted-by":"crossref","first-page":"a018713","DOI":"10.1101\/cshperspect.a018713","article-title":"Erasers of histone acetylation: the histone deacetylase enzymes","volume":"6","author":"Seto","year":"2014","journal-title":"Cold Spring Harb. Perspect. Biol."},{"issue":"6","key":"10.1016\/j.bone.2020.115606_bb0045","doi-asserted-by":"crossref","first-page":"1599","DOI":"10.1016\/S1097-2765(03)00186-2","article-title":"Histones are first hyperacetylated and then lose contact with the activated PHO5 promoter","volume":"11","author":"Reinke","year":"2003","journal-title":"Mol. Cell"},{"issue":"6735","key":"10.1016\/j.bone.2020.115606_bb0050","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1038\/20974","article-title":"Structure and ligand of a histone acetyltransferase bromodomain","volume":"399","author":"Dhalluin","year":"1999","journal-title":"Nature"},{"issue":"6649","key":"10.1016\/j.bone.2020.115606_bb0055","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1038\/38664","article-title":"Histone acetylation in chromatin structure and transcription","volume":"389","author":"Grunstein","year":"1997","journal-title":"Nature"},{"issue":"6765","key":"10.1016\/j.bone.2020.115606_bb0060","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1038\/47412","article-title":"The language of covalent histone modifications","volume":"403","author":"Strahl","year":"2000","journal-title":"Nature"},{"issue":"6","key":"10.1016\/j.bone.2020.115606_bb0065","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1038\/nrg3454","article-title":"Exploring the three-dimensional organization of genomes: interpreting chromatin interaction data","volume":"14","author":"Dekker","year":"2013","journal-title":"Nat Rev Genet"},{"issue":"9","key":"10.1016\/j.bone.2020.115606_bb0070","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1038\/nrd4360","article-title":"Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders","volume":"13","author":"Falkenberg","year":"2014","journal-title":"Nat. Rev. Drug Discov."},{"issue":"1","key":"10.1016\/j.bone.2020.115606_bb0075","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1089\/ars.2013.5776","article-title":"Targeting histone deacetylases in diseases: where are we?","volume":"23","author":"Benedetti","year":"2015","journal-title":"Antioxid. Redox Signal."},{"issue":"4","key":"10.1016\/j.bone.2020.115606_bb0080","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1007\/s11154-010-9153-1","article-title":"Cellular mechanisms of bone remodeling","volume":"11","author":"Eriksen","year":"2010","journal-title":"Rev. Endocr. Metab. Disord."},{"issue":"9","key":"10.1016\/j.bone.2020.115606_bb0085","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1038\/nrendo.2013.137","article-title":"Osteopetrosis: genetics, treatment and new insights into osteoclast function","volume":"9","author":"Sobacchi","year":"2013","journal-title":"Nat Rev Endocrinol"},{"key":"10.1016\/j.bone.2020.115606_bb0090","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1146\/annurev-pathol-011110-130203","article-title":"Disorders of bone remodeling","volume":"6","author":"Feng","year":"2011","journal-title":"Annu. Rev. Pathol."},{"issue":"25","key":"10.1016\/j.bone.2020.115606_bb0095","doi-asserted-by":"crossref","first-page":"13708","DOI":"10.1073\/pnas.250477697","article-title":"Genomewide studies of histone deacetylase function in yeast","volume":"97","author":"Bernstein","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"Pt 3","key":"10.1016\/j.bone.2020.115606_bb0100","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1042\/bj20021321","article-title":"Histone deacetylases (HDACs): characterization of the classical HDAC family","volume":"370","author":"de Ruijter","year":"2003","journal-title":"Biochem. J."},{"issue":"1","key":"10.1016\/j.bone.2020.115606_bb0105","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.jmb.2004.02.006","article-title":"Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis","volume":"338","author":"Gregoretti","year":"2004","journal-title":"J. Mol. Biol."},{"issue":"4","key":"10.1016\/j.bone.2020.115606_bb0110","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/S0092-8674(02)00746-8","article-title":"Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases","volume":"109","author":"Robyr","year":"2002","journal-title":"Cell"},{"issue":"2","key":"10.1016\/j.bone.2020.115606_bb0115","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/S0959-437X(03)00015-7","article-title":"Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression","volume":"13","author":"Yang","year":"2003","journal-title":"Curr. Opin. Genet. Dev."},{"issue":"18","key":"10.1016\/j.bone.2020.115606_bb0120","doi-asserted-by":"crossref","first-page":"6091","DOI":"10.1128\/MCB.21.18.6091-6101.2001","article-title":"The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3","volume":"21","author":"Guenther","year":"2001","journal-title":"Mol. Cell. Biol."},{"issue":"2","key":"10.1016\/j.bone.2020.115606_bb0125","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1128\/MCB.23.2.607-619.2003","article-title":"The inv(16) fusion protein associates with corepressors via a smooth muscle myosin heavy-chain domain","volume":"23","author":"Durst","year":"2003","journal-title":"Mol. Cell. Biol."},{"issue":"4","key":"10.1016\/j.bone.2020.115606_bb0130","doi-asserted-by":"crossref","first-page":"1359","DOI":"10.1152\/physrev.00004.2015","article-title":"Histone deacetylases in bone development and skeletal disorders","volume":"95","author":"Bradley","year":"2015","journal-title":"Physiol. Rev."},{"issue":"2","key":"10.1016\/j.bone.2020.115606_bb0135","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/S1534-5807(01)00003-X","article-title":"The transcription factors L-Sox5 and Sox6 are essential for cartilage formation","volume":"1","author":"Smits","year":"2001","journal-title":"Dev. Cell"},{"issue":"4","key":"10.1016\/j.bone.2020.115606_bb0140","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1002\/(SICI)1097-0177(199904)214:4<279::AID-AJA1>3.0.CO;2-W","article-title":"Maturational disturbance of chondrocytes in Cbfa1-deficient mice","volume":"214","author":"Inada","year":"1999","journal-title":"Dev. Dyn."},{"issue":"1","key":"10.1016\/j.bone.2020.115606_bb0145","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1083\/jcb.153.1.87","article-title":"Skeletal malformations caused by overexpression of Cbfa1 or its dominant negative form in chondrocytes","volume":"153","author":"Ueta","year":"2001","journal-title":"J. Cell Biol."},{"issue":"5","key":"10.1016\/j.bone.2020.115606_bb0150","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1016\/S0092-8674(00)80258-5","article-title":"Targeted disruption of Cbfa1 results in a complete lack of bone formation owing to maturational arrest of osteoblasts","volume":"89","author":"Komori","year":"1997","journal-title":"Cell"},{"issue":"5","key":"10.1016\/j.bone.2020.115606_bb0155","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1016\/S0092-8674(00)80259-7","article-title":"Cbfa1, a candidate gene for cleidocranial dysplasia syndrome, is essential for osteoblast differentiation and bone development","volume":"89","author":"Otto","year":"1997","journal-title":"Cell"},{"issue":"1","key":"10.1016\/j.bone.2020.115606_bb0160","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/S0092-8674(01)00622-5","article-title":"The novel zinc finger-containing transcription factor osterix is required for osteoblast differentiation and bone formation","volume":"108","author":"Nakashima","year":"2002","journal-title":"Cell"},{"key":"10.1016\/j.bone.2020.115606_bb0165","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.bone.2015.04.035","article-title":"Bone development","volume":"80","author":"Berendsen","year":"2015","journal-title":"Bone"},{"issue":"10","key":"10.1016\/j.bone.2020.115606_bb0170","doi-asserted-by":"crossref","first-page":"2432","DOI":"10.1210\/me.2006-0061","article-title":"Histone deacetylase 1-mediated histone modification regulates osteoblast differentiation","volume":"20","author":"Lee","year":"2006","journal-title":"Mol. Endocrinol."},{"issue":"12","key":"10.1016\/j.bone.2020.115606_bb0175","doi-asserted-by":"crossref","first-page":"2254","DOI":"10.1359\/JBMR.050813","article-title":"Histone deacetylase inhibitors promote osteoblast maturation","volume":"20","author":"Schroeder","year":"2005","journal-title":"J. Bone Miner. Res."},{"issue":"11","key":"10.1016\/j.bone.2020.115606_bb0180","doi-asserted-by":"crossref","first-page":"2672","DOI":"10.1093\/emboj\/21.11.2672","article-title":"Essential function of histone deacetylase 1 in proliferation control and CDK inhibitor repression","volume":"21","author":"Lagger","year":"2002","journal-title":"EMBO J."},{"issue":"15","key":"10.1016\/j.bone.2020.115606_bb0185","doi-asserted-by":"crossref","first-page":"1990","DOI":"10.1101\/gad.1008002","article-title":"Shh establishes an Nkx3.2\/Sox9 autoregulatory loop that is maintained by BMP signals to induce somitic chondrogenesis","volume":"16","author":"Zeng","year":"2002","journal-title":"Genes Dev."},{"issue":"3","key":"10.1016\/j.bone.2020.115606_bb0190","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/S1534-5807(01)00039-9","article-title":"The chick transcriptional repressor Nkx3.2 acts downstream of Shh to promote BMP-dependent axial chondrogenesis","volume":"1","author":"Murtaugh","year":"2001","journal-title":"Dev. Cell"},{"issue":"10","key":"10.1016\/j.bone.2020.115606_bb0195","doi-asserted-by":"crossref","first-page":"3539","DOI":"10.1096\/fj.09-133215","article-title":"A novel domain in histone deacetylase 1 and 2 mediates repression of cartilage-specific genes in human chondrocytes","volume":"23","author":"Hong","year":"2009","journal-title":"FASEB J."},{"issue":"45","key":"10.1016\/j.bone.2020.115606_bb0200","doi-asserted-by":"crossref","first-page":"47081","DOI":"10.1074\/jbc.M405288200","article-title":"Leukemia\/lymphoma-related factor, a POZ domain-containing transcriptional repressor, interacts with histone deacetylase-1 and inhibits cartilage oligomeric matrix protein gene expression and chondrogenesis","volume":"279","author":"Liu","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"23","key":"10.1016\/j.bone.2020.115606_bb0205","doi-asserted-by":"crossref","first-page":"17123","DOI":"10.1074\/jbc.M700599200","article-title":"Regulation of type II collagen expression by histone deacetylase in articular chondrocytes","volume":"282","author":"Huh","year":"2007","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.bone.2020.115606_bb0210","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1038\/nm1552","article-title":"Hdac2 regulates the cardiac hypertrophic response by modulating Gsk3 beta activity","volume":"13","author":"Trivedi","year":"2007","journal-title":"Nat. Med."},{"issue":"2","key":"10.1016\/j.bone.2020.115606_bb0215","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1038\/s41580-018-0076-0","article-title":"Integrative regulation of physiology by histone deacetylase 3","volume":"20","author":"Emmett","year":"2019","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"11","key":"10.1016\/j.bone.2020.115606_bb0220","doi-asserted-by":"crossref","first-page":"1240","DOI":"10.1161\/CIRCRESAHA.111.255067","article-title":"Histone deacetylase 3 regulates smooth muscle differentiation in neural crest cells and development of the cardiac outflow tract","volume":"109","author":"Singh","year":"2011","journal-title":"Circ. Res."},{"issue":"2","key":"10.1016\/j.bone.2020.115606_bb0225","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/j.ydbio.2013.03.008","article-title":"Murine craniofacial development requires Hdac3-mediated repression of Msx gene expression","volume":"377","author":"Singh","year":"2013","journal-title":"Dev. Biol."},{"issue":"7","key":"10.1016\/j.bone.2020.115606_bb0230","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0011492","article-title":"Histone deacetylase 3 depletion in osteo\/chondroprogenitor cells decreases bone density and increases marrow fat","volume":"5","author":"Razidlo","year":"2010","journal-title":"PLoS One"},{"issue":"1","key":"10.1016\/j.bone.2020.115606_bb0235","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1080\/03008207.2016.1236088","article-title":"Histone deacetylase 3 suppresses Erk phosphorylation and matrix metalloproteinase (Mmp)-13 activity in chondrocytes","volume":"58","author":"Carpio","year":"2017","journal-title":"Connect. Tissue Res."},{"issue":"440","key":"10.1016\/j.bone.2020.115606_bb0240","doi-asserted-by":"crossref","DOI":"10.1126\/scisignal.aaf3273","article-title":"Histone deacetylase 3 supports endochondral bone formation by controlling cytokine signaling and matrix remodeling","volume":"9","author":"Carpio","year":"2016","journal-title":"Sci Signal"},{"issue":"1","key":"10.1016\/j.bone.2020.115606_bb0245","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1016\/j.bone.2012.10.015","article-title":"Histone deacetylase 3 is required for maintenance of bone mass during aging","volume":"52","author":"McGee-Lawrence","year":"2013","journal-title":"Bone"},{"issue":"4","key":"10.1016\/j.bone.2020.115606_bb0250","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1016\/j.cell.2004.10.024","article-title":"Histone deacetylase 4 controls chondrocyte hypertrophy during skeletogenesis","volume":"119","author":"Vega","year":"2004","journal-title":"Cell"},{"issue":"5","key":"10.1016\/j.bone.2020.115606_bb0255","doi-asserted-by":"crossref","DOI":"10.1172\/jci.insight.97903","article-title":"PTHrP targets HDAC4 and HDAC5 to repress chondrocyte hypertrophy","volume":"4","author":"Nishimori","year":"2019","journal-title":"JCI Insight"},{"issue":"7","key":"10.1016\/j.bone.2020.115606_bb0260","doi-asserted-by":"crossref","first-page":"1362","DOI":"10.1002\/jbmr.3422","article-title":"The deletion of Hdac4 in mouse osteoblasts influences both catabolic and anabolic effects in bone","volume":"33","author":"Nakatani","year":"2018","journal-title":"J. Bone Miner. Res."},{"issue":"6","key":"10.1016\/j.bone.2020.115606_bb0265","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1083\/jcb.201403138","article-title":"HDAC4 integrates PTH and sympathetic signaling in osteoblasts","volume":"205","author":"Obri","year":"2014","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bone.2020.115606_bb0270","doi-asserted-by":"crossref","first-page":"13176","DOI":"10.1038\/ncomms13176","article-title":"SIKs control osteocyte responses to parathyroid hormone","volume":"7","author":"Wein","year":"2016","journal-title":"Nat. Commun."},{"issue":"3","key":"10.1016\/j.bone.2020.115606_bb0275","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1002\/jbmr.2381","article-title":"HDAC5 controls MEF2C-driven sclerostin expression in osteocytes","volume":"30","author":"Wein","year":"2015","journal-title":"J. Bone Miner. Res."},{"issue":"1","key":"10.1016\/j.bone.2020.115606_bb0280","doi-asserted-by":"crossref","first-page":"3282","DOI":"10.1038\/s41467-020-17099-3","article-title":"A FAK\/HDAC5 signaling axis controls osteocyte mechanotransduction","volume":"11","author":"Sato","year":"2020","journal-title":"Nat. Commun."},{"issue":"2","key":"10.1016\/j.bone.2020.115606_bb0285","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/j.cell.2006.05.040","article-title":"Histone deacetylase 7 maintains vascular integrity by repressing matrix metalloproteinase 10","volume":"126","author":"Chang","year":"2006","journal-title":"Cell"},{"issue":"1","key":"10.1016\/j.bone.2020.115606_bb0290","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1074\/jbc.M114.596247","article-title":"Histone deacetylase 7 (Hdac7) suppresses chondrocyte proliferation and beta-catenin activity during endochondral ossification","volume":"290","author":"Bradley","year":"2015","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.bone.2020.115606_bb0295","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1210\/me.2012-1302","article-title":"HDAC7 inhibits osteoclastogenesis by reversing RANKL-triggered beta-catenin switch","volume":"27","author":"Jin","year":"2013","journal-title":"Mol. Endocrinol."},{"key":"10.1016\/j.bone.2020.115606_bb0300","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.biocel.2014.07.003","article-title":"Histone deacetylase 8 suppresses osteogenic differentiation of bone marrow stromal cells by inhibiting histone H3K9 acetylation and RUNX2 activity","volume":"54","author":"Fu","year":"2014","journal-title":"Int. J. Biochem. Cell Biol."},{"issue":"5","key":"10.1016\/j.bone.2020.115606_bb0305","doi-asserted-by":"crossref","first-page":"730","DOI":"10.1210\/me.2014-1365","article-title":"HDAC9 inhibits osteoclastogenesis via mutual suppression of PPARgamma\/RANKL signaling","volume":"29","author":"Jin","year":"2015","journal-title":"Mol. Endocrinol."},{"key":"10.1016\/j.bone.2020.115606_bb0310","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1177\/1087057111422103","article-title":"Sirtuin 1 (SIRT1): the misunderstood HDAC","volume":"16","author":"St\u00fcnkel","year":"2011","journal-title":"J. Biomol. Screen."},{"key":"10.1016\/j.bone.2020.115606_bb0315","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1128\/MCB.23.1.38-54.2003","article-title":"The mammalian SIR2 protein has a role in embryogenesis and gametogenesis","volume":"23","author":"McBurney","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bone.2020.115606_bb0320","doi-asserted-by":"crossref","first-page":"1097","DOI":"10.1016\/j.mad.2005.04.006","article-title":"The Sirt1 deacetylase modulates the insulin-like growth factor signaling pathway in mammals","volume":"126","author":"Lemieux","year":"2005","journal-title":"Mech. Ageing Dev."},{"key":"10.1016\/j.bone.2020.115606_bb0325","doi-asserted-by":"crossref","first-page":"5871","DOI":"10.3390\/nu6125871","article-title":"Effects of resveratrol supplementation on bone growth in young rats and microarchitecture and remodeling in ageing rats","volume":"6","author":"Lee","year":"2014","journal-title":"Nutrients"},{"key":"10.1016\/j.bone.2020.115606_bb0330","doi-asserted-by":"crossref","first-page":"1474","DOI":"10.1016\/j.jnutbio.2011.09.010","article-title":"MicroRNAs in the growth plate are responsive to nutritional cues: association between miR-140 and SIRT1","volume":"23","author":"Pando","year":"2012","journal-title":"Journal of Nutritional Biochemistry"},{"key":"10.1016\/j.bone.2020.115606_bb0335","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.pone.0185236","article-title":"SIRT1 is a positive regulator of in vivo bone mass and a therapeutic target for osteoporosis","volume":"12","author":"Zainabadi","year":"2017","journal-title":"PLoS One"},{"key":"10.1016\/j.bone.2020.115606_bb0340","doi-asserted-by":"crossref","first-page":"960","DOI":"10.1002\/jbmr.1824","article-title":"Silent information regulator (sir)T1 inhibits NF-\u03baB signaling to maintain normal skeletal remodeling","volume":"28","author":"Edwards","year":"2013","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bone.2020.115606_bb0345","doi-asserted-by":"crossref","first-page":"24069","DOI":"10.1074\/jbc.M114.561803","article-title":"Sirtuin1 (Sirt1) promotes cortical bone formation by preventing \u03b2-catenin sequestration by FoxO transcription factors in osteoblast progenitors","volume":"289","author":"Iyer","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bone.2020.115606_bb0350","doi-asserted-by":"crossref","first-page":"4514","DOI":"10.1210\/en.2011-1128","article-title":"Sirt1 is a regulator of bone mass and a repressor of sost encoding for sclerostin, a bone formation inhibitor","volume":"152","author":"Cohen-Kfir","year":"2011","journal-title":"Endocrinology"},{"key":"10.1016\/j.bone.2020.115606_bb0355","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1111\/acel.12220","article-title":"SRT2104 extends survival of male mice on a standard diet and preserves bone and muscle mass","volume":"13","author":"Mercken","year":"2014","journal-title":"Aging Cell"},{"key":"10.1016\/j.bone.2020.115606_bb0360","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1002\/ar.1090490408","article-title":"Mitochondria in osteoclasts","volume":"49","author":"Ch\u2019uan","year":"1931","journal-title":"Anat. Rec."},{"key":"10.1016\/j.bone.2020.115606_bb0365","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1002\/jbmr.2974","article-title":"SOD2 and Sirt3 control osteoclastogenesis by regulating mitochondrial ROS","volume":"32","author":"Kim","year":"2017","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bone.2020.115606_bb0370","doi-asserted-by":"crossref","first-page":"2741","DOI":"10.1210\/en.2016-1739","article-title":"Sirtuin-3 promotes adipogenesis, osteoclastogenesis, and bone loss in aging male mice","volume":"158","author":"Ho","year":"2017","journal-title":"Endocrinology"},{"key":"10.1016\/j.bone.2020.115606_bb0375","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.tem.2016.10.002","article-title":"SIRT6: novel mechanisms and links to aging and disease","volume":"28","author":"Tasselli","year":"2017","journal-title":"Trends in Endocrinology & Metabolism"},{"key":"10.1016\/j.bone.2020.115606_bb0380","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1016\/0140-6736(92)92240-G","article-title":"Ultrasonographically detectable markers of fetal chromosomal abnoormalities","volume":"340","author":"Nicolaides","year":"1992","journal-title":"Lancet"},{"key":"10.1016\/j.bone.2020.115606_bb0385","first-page":"1","article-title":"SIRT6 promotes osteogenic differentiation of mesenchymal stem cells through BMP signaling","volume":"7","author":"Zhang","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bone.2020.115606_bb0390","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.bone.2015.07.018","article-title":"SIRT6 deficiency culminates in low-turnover osteopenia","volume":"81","author":"Sugatani","year":"2015","journal-title":"Bone"},{"key":"10.1016\/j.bone.2020.115606_bb0395","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1002\/biof.1320","article-title":"Sirtuin 6 suppresses hypoxia-induced inflammatory response in human osteoblasts via inhibition of reactive oxygen species production and glycolysis\u2014a therapeutic implication in inflammatory bone resorption","volume":"43","author":"Hou","year":"2017","journal-title":"BioFactors"},{"key":"10.1016\/j.bone.2020.115606_bb0400","first-page":"1","article-title":"Evidence for excessive osteoclast activation in SIRT6 null mice","volume":"8","author":"Zhang","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bone.2020.115606_bb0405","doi-asserted-by":"crossref","DOI":"10.1038\/cddis.2017.429","article-title":"Knockdown of SIRT7 enhances the osteogenic differentiation of human bone marrow mesenchymal stem cells partly via activation of the Wnt\/\u03b2-catenin signaling pathway","volume":"8","author":"Chen","year":"2017","journal-title":"Cell Death Dis."},{"issue":"5","key":"10.1016\/j.bone.2020.115606_bb0410","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1002\/ajmg.a.61101","article-title":"A de novo HDAC2 variant in a patient with features consistent with Cornelia de Lange syndrome phenotype","volume":"179","author":"Wagner","year":"2019","journal-title":"Am. J. Med. Genet. A"},{"issue":"2","key":"10.1016\/j.bone.2020.115606_bb0415","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.ajhg.2010.07.011","article-title":"Haploinsufficiency of HDAC4 causes brachydactyly mental retardation syndrome, with brachydactyly type E, developmental delays, and behavioral problems","volume":"87","author":"Williams","year":"2010","journal-title":"Am. J. Hum. Genet."},{"issue":"11","key":"10.1016\/j.bone.2020.115606_bb0420","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1038\/ng.446","article-title":"Twenty bone-mineral-density loci identified by large-scale meta-analysis of genome-wide association studies","volume":"41","author":"Rivadeneira","year":"2009","journal-title":"Nat. Genet."},{"issue":"7415","key":"10.1016\/j.bone.2020.115606_bb0425","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1038\/nature11316","article-title":"HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle","volume":"489","author":"Deardorff","year":"2012","journal-title":"Nature"},{"issue":"11","key":"10.1016\/j.bone.2020.115606_bb0430","doi-asserted-by":"crossref","first-page":"2888","DOI":"10.1093\/hmg\/ddu002","article-title":"Loss-of-function HDAC8 mutations cause a phenotypic spectrum of Cornelia de Lange syndrome-like features, ocular hypertelorism, large fontanelle and X-linked inheritance","volume":"23","author":"Kaiser","year":"2014","journal-title":"Hum. Mol. Genet."},{"issue":"9","key":"10.1016\/j.bone.2020.115606_bb0435","doi-asserted-by":"crossref","first-page":"2157","DOI":"10.1021\/cb5003762","article-title":"Compromised structure and function of HDAC8 mutants identified in Cornelia de Lange syndrome spectrum disorders","volume":"9","author":"Decroos","year":"2014","journal-title":"ACS Chem. Biol."},{"issue":"8","key":"10.1016\/j.bone.2020.115606_bb0440","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1136\/jmedgenet-2012-100921","article-title":"X-exome sequencing identifies a HDAC8 variant in a large pedigree with X-linked intellectual disability, truncal obesity, gynaecomastia, hypogonadism and unusual face","volume":"49","author":"Harakalova","year":"2012","journal-title":"J. Med. Genet."},{"issue":"11","key":"10.1016\/j.bone.2020.115606_bb0445","doi-asserted-by":"crossref","first-page":"1580","DOI":"10.1038\/s41588-019-0514-8","article-title":"HDAC9 is implicated in atherosclerotic aortic calcification and affects vascular smooth muscle cell phenotype","volume":"51","author":"Malhotra","year":"2019","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bone.2020.115606_bb0450","doi-asserted-by":"crossref","first-page":"1498","DOI":"10.1210\/me.2015-1133","article-title":"Sirtuin1 suppresses osteoclastogenesis by deacetylating foxos","volume":"29","author":"Kim","year":"2015","journal-title":"Mol. Endocrinol."},{"key":"10.1016\/j.bone.2020.115606_bb0455","doi-asserted-by":"crossref","first-page":"2373","DOI":"10.1007\/s00198-016-3536-4","article-title":"Reduced Sirtuin1 expression at the femoral neck in women who sustained an osteoporotic hip fracture","volume":"27","author":"El-Haj","year":"2016","journal-title":"Osteoporos. Int."},{"key":"10.1016\/j.bone.2020.115606_bb0460","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1101\/gad.307330.117","article-title":"An inactivating mutation in the histone deacetylase SIRT6 causes human perinatal lethality","volume":"32","author":"Ferrer","year":"2018","journal-title":"Genes Dev."},{"issue":"14","key":"10.1016\/j.bone.2020.115606_bb0465","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1101\/gad.1809209","article-title":"Epigenetic control of skull morphogenesis by histone deacetylase 8","volume":"23","author":"Haberland","year":"2009","journal-title":"Genes Dev."},{"key":"10.1016\/j.bone.2020.115606_bb0470","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1146\/annurev-physiol-021119-034332","article-title":"The osteocyte: new insights","volume":"82","author":"Robling","year":"2020","journal-title":"Annu. Rev. Physiol."},{"issue":"1","key":"10.1016\/j.bone.2020.115606_bb0475","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/j.bone.2007.09.047","article-title":"Osteocytes as mechanosensors in the inhibition of bone resorption due to mechanical loading","volume":"42","author":"You","year":"2008","journal-title":"Bone"},{"issue":"10","key":"10.1016\/j.bone.2020.115606_bb0480","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1038\/nm.2452","article-title":"Evidence for osteocyte regulation of bone homeostasis through RANKL expression","volume":"17","author":"Nakashima","year":"2011","journal-title":"Nat. Med."},{"issue":"23","key":"10.1016\/j.bone.2020.115606_bb0485","doi-asserted-by":"crossref","first-page":"6267","DOI":"10.1093\/emboj\/cdg599","article-title":"Osteocyte control of bone formation via sclerostin, a novel BMP antagonist","volume":"22","author":"Winkler","year":"2003","journal-title":"EMBO J."},{"issue":"13","key":"10.1016\/j.bone.2020.115606_bb0490","doi-asserted-by":"crossref","first-page":"1842","DOI":"10.1096\/fj.05-4221fje","article-title":"Sclerostin is a delayed secreted product of osteocytes that inhibits bone formation","volume":"19","author":"Poole","year":"2005","journal-title":"FASEB J."},{"issue":"36","key":"10.1016\/j.bone.2020.115606_bb0495","doi-asserted-by":"crossref","first-page":"24995","DOI":"10.1074\/jbc.M114.564997","article-title":"Class I and IIa histone deacetylases have opposite effects on sclerostin gene regulation","volume":"289","author":"Baertschi","year":"2014","journal-title":"J. Biol. Chem."},{"issue":"6937","key":"10.1016\/j.bone.2020.115606_bb0500","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1038\/nature01658","article-title":"Osteoclast differentiation and activation","volume":"423","author":"Boyle","year":"2003","journal-title":"Nature"},{"issue":"7","key":"10.1016\/j.bone.2020.115606_bb0505","doi-asserted-by":"crossref","first-page":"3597","DOI":"10.1073\/pnas.95.7.3597","article-title":"Osteoclast differentiation factor is a ligand for osteoprotegerin\/osteoclastogenesis-inhibitory factor and is identical to TRANCE\/RANKL","volume":"95","author":"Yasuda","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"2","key":"10.1016\/j.bone.2020.115606_bb0510","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/S0092-8674(00)81569-X","article-title":"Osteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation","volume":"93","author":"Lacey","year":"1998","journal-title":"Cell"},{"issue":"11","key":"10.1016\/j.bone.2020.115606_bb0515","doi-asserted-by":"crossref","first-page":"4018","DOI":"10.1128\/MCB.01839-06","article-title":"Eos, MITF, and PU.1 recruit corepressors to osteoclast-specific genes in committed myeloid progenitors","volume":"27","author":"Hu","year":"2007","journal-title":"Mol. Cell. Biol."},{"issue":"10","key":"10.1016\/j.bone.2020.115606_bb0520","doi-asserted-by":"crossref","first-page":"C780","DOI":"10.1152\/ajpcell.00351.2015","article-title":"HDAC2 regulates FoxO1 during RANKL-induced osteoclastogenesis","volume":"310","author":"Dou","year":"2016","journal-title":"Am J Physiol Cell Physiol"},{"issue":"14","key":"10.1016\/j.bone.2020.115606_bb0525","doi-asserted-by":"crossref","first-page":"12056","DOI":"10.1074\/jbc.M110.216853","article-title":"HDAC3 and HDAC7 have opposite effects on osteoclast differentiation","volume":"286","author":"Pham","year":"2011","journal-title":"J. Biol. Chem."},{"issue":"28","key":"10.1016\/j.bone.2020.115606_bb0530","doi-asserted-by":"crossref","first-page":"2429","DOI":"10.2174\/1568026619666181129141822","article-title":"Structure, functions and selective inhibitors of HDAC6","volume":"18","author":"Liang","year":"2018","journal-title":"Curr. Top. Med. Chem."},{"issue":"2","key":"10.1016\/j.bone.2020.115606_bb0535","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1038\/s41368-019-0053-2","article-title":"Harnessing the HDAC-histone deacetylase enzymes, inhibitors and how these can be utilised in tissue engineering","volume":"11","author":"Lawlor","year":"2019","journal-title":"Int J Oral Sci"},{"issue":"4","key":"10.1016\/j.bone.2020.115606_bb0540","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1016\/j.bbrc.2004.01.152","article-title":"Trichostatin A activates the osteopontin gene promoter through AP1 site","volume":"315","author":"Sakata","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"11","key":"10.1016\/j.bone.2020.115606_bb0545","doi-asserted-by":"crossref","first-page":"1631","DOI":"10.1016\/0020-711X(93)90522-G","article-title":"Effects of short chain fatty acid, sodium butyrate, on osteoblastic cells and osteoclastic cells","volume":"25","author":"Iwami","year":"1993","journal-title":"Int. J. BioChemiPhysics"},{"issue":"3","key":"10.1016\/j.bone.2020.115606_bb0550","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1021\/ml1002794","article-title":"In vitro and in vivo osteogenic activity of Largazole","volume":"2","author":"Lee","year":"2011","journal-title":"ACS Med. Chem. Lett."},{"issue":"12","key":"10.1016\/j.bone.2020.115606_bb0555","doi-asserted-by":"crossref","first-page":"3233","DOI":"10.1002\/jcp.22684","article-title":"Inhibitors of histone deacetylases in class I and class II suppress human osteoclasts in vitro","volume":"226","author":"Cantley","year":"2011","journal-title":"J. Cell. Physiol."},{"issue":"3459","key":"10.1016\/j.bone.2020.115606_bb0560","doi-asserted-by":"crossref","first-page":"3451","DOI":"10.1182\/blood-2002-08-2622","article-title":"Two histone deacetylase inhibitors, trichostatin A and sodium butyrate, suppress differentiation into osteoclasts but not into macrophages","volume":"101","author":"Rahman","year":"2003","journal-title":"Blood"},{"issue":"9","key":"10.1016\/j.bone.2020.115606_bb0565","doi-asserted-by":"crossref","first-page":"1713","DOI":"10.1093\/rheumatology\/kev022","article-title":"Inhibiting histone deacetylase 1 suppresses both inflammation and bone loss in arthritis","volume":"54","author":"Cantley","year":"2015","journal-title":"Rheumatology (Oxford)"},{"issue":"9","key":"10.1016\/j.bone.2020.115606_bb0570","doi-asserted-by":"crossref","first-page":"5809","DOI":"10.4049\/jimmunol.175.9.5809","article-title":"Inhibition of histone deacetylase suppresses osteoclastogenesis and bone destruction by inducing IFN-beta production","volume":"175","author":"Nakamura","year":"2005","journal-title":"J. Immunol."},{"issue":"1","key":"10.1016\/j.bone.2020.115606_bb0575","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1038\/nrg2485","article-title":"The many roles of histone deacetylases in development and physiology: implications for disease and therapy","volume":"10","author":"Haberland","year":"2009","journal-title":"Nat Rev Genet"},{"issue":"3","key":"10.1016\/j.bone.2020.115606_bb0580","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1074\/mcp.O114.046565","article-title":"Post-translational modifications regulate class IIa histone deacetylase (HDAC) function in health and disease","volume":"14","author":"Mathias","year":"2015","journal-title":"Mol. Cell. Proteomics"},{"issue":"44","key":"10.1016\/j.bone.2020.115606_bb0585","doi-asserted-by":"crossref","first-page":"17335","DOI":"10.1073\/pnas.0706487104","article-title":"Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases","volume":"104","author":"Lahm","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"5","key":"10.1016\/j.bone.2020.115606_bb0590","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1038\/nchembio.1223","article-title":"Selective class IIa histone deacetylase inhibition via a nonchelating zinc-binding group","volume":"9","author":"Lobera","year":"2013","journal-title":"Nat. Chem. Biol."},{"issue":"3","key":"10.1016\/j.bone.2020.115606_bb0595","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1016\/j.devcel.2007.02.004","article-title":"MEF2C transcription factor controls chondrocyte hypertrophy and bone development","volume":"12","author":"Arnold","year":"2007","journal-title":"Dev. Cell"},{"key":"10.1016\/j.bone.2020.115606_bb0600","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1016\/j.bone.2016.06.010","article-title":"MMP-13 is one of the critical mediators of the effect of HDAC4 deletion on the skeleton","volume":"90","author":"Nakatani","year":"2016","journal-title":"Bone"},{"issue":"8","key":"10.1016\/j.bone.2020.115606_bb0605","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0006612","article-title":"Loss of the putative catalytic domain of HDAC4 leads to reduced thermal nociception and seizures while allowing normal bone development","volume":"4","author":"Rajan","year":"2009","journal-title":"PLoS One"},{"issue":"2","key":"10.1016\/j.bone.2020.115606_bb0610","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1016\/j.bone.2012.09.040","article-title":"In vitro and in vivo approaches to study osteocyte biology","volume":"54","author":"Kalajzic","year":"2013","journal-title":"Bone"},{"issue":"4","key":"10.1016\/j.bone.2020.115606_bb0615","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1177\/154405910708600404","article-title":"DMP1-targeted Cre expression in odontoblasts and osteocytes","volume":"86","author":"Lu","year":"2007","journal-title":"J. Dent. Res."},{"issue":"10","key":"10.1016\/j.bone.2020.115606_bb0620","doi-asserted-by":"crossref","first-page":"3437","DOI":"10.1128\/MCB.01611-07","article-title":"Histone deacetylase 5 acquires calcium\/calmodulin-dependent kinase II responsiveness by oligomerization with histone deacetylase 4","volume":"28","author":"Backs","year":"2008","journal-title":"Mol. Cell. Biol."},{"issue":"1","key":"10.1016\/j.bone.2020.115606_bb0625","doi-asserted-by":"crossref","first-page":"3469","DOI":"10.1038\/s41467-019-11409-0","article-title":"Class IIa HDACs regulate learning and memory through dynamic experience-dependent repression of transcription","volume":"10","author":"Zhu","year":"2019","journal-title":"Nat. Commun."},{"issue":"19","key":"10.1016\/j.bone.2020.115606_bb0630","doi-asserted-by":"crossref","first-page":"8467","DOI":"10.1128\/MCB.24.19.8467-8476.2004","article-title":"Histone deacetylases 5 and 9 govern responsiveness of the heart to a subset of stress signals and play redundant roles in heart development","volume":"24","author":"Chang","year":"2004","journal-title":"Mol. Cell. Biol."},{"issue":"2","key":"10.1016\/j.bone.2020.115606_bb0635","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1038\/nm.3074","article-title":"WNT signaling in bone homeostasis and disease: from human mutations to treatments","volume":"19","author":"Baron","year":"2013","journal-title":"Nat. Med."},{"issue":"3","key":"10.1016\/j.bone.2020.115606_bb0640","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1359\/jbmr.071104","article-title":"Histone deacetylase 7 associates with Runx2 and represses its activity during osteoblast maturation in a deacetylation-independent manner","volume":"23","author":"Jensen","year":"2008","journal-title":"J. Bone Miner. Res."},{"issue":"4","key":"10.1016\/j.bone.2020.115606_bb0645","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0123843","article-title":"Deletion of histone deacetylase 7 in osteoclasts decreases bone mass in mice by interactions with MITF","volume":"10","author":"Stemig","year":"2015","journal-title":"PLoS One"},{"issue":"4","key":"10.1016\/j.bone.2020.115606_bb0650","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1016\/S1097-2765(01)00360-4","article-title":"Linkage of M-CSF signaling to Mitf, TFE3, and the osteoclast defect in Mitf(mi\/mi) mice","volume":"8","author":"Weilbaecher","year":"2001","journal-title":"Mol. Cell"},{"issue":"2","key":"10.1016\/j.bone.2020.115606_bb0655","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/j.stem.2016.10.005","article-title":"Cardiac fibroblasts adopt Osteogenic fates and can be targeted to attenuate pathological heart calcification","volume":"20","author":"Pillai","year":"2017","journal-title":"Cell Stem Cell"},{"issue":"22","key":"10.1016\/j.bone.2020.115606_bb0660","doi-asserted-by":"crossref","first-page":"115087","DOI":"10.1016\/j.bmc.2019.115087","article-title":"Recent advances in class IIa histone deacetylases research","volume":"27","author":"Asfaha","year":"2019","journal-title":"Bioorg. Med. Chem."},{"issue":"6937","key":"10.1016\/j.bone.2020.115606_bb0665","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1038\/nature01657","article-title":"Developmental regulation of the growth plate","volume":"423","author":"Kronenberg","year":"2003","journal-title":"Nature"},{"issue":"21","key":"10.1016\/j.bone.2020.115606_bb0670","doi-asserted-by":"crossref","first-page":"5751","DOI":"10.1128\/MCB.00415-09","article-title":"Parathyroid hormone-related peptide represses chondrocyte hypertrophy through a protein phosphatase 2A\/histone deacetylase 4\/MEF2 pathway","volume":"29","author":"Kozhemyakina","year":"2009","journal-title":"Mol. Cell. Biol."},{"issue":"5","key":"10.1016\/j.bone.2020.115606_bb0675","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1038\/nm1573","article-title":"SIK1 is a class II HDAC kinase that promotes survival of skeletal myocytes","volume":"13","author":"Berdeaux","year":"2007","journal-title":"Nat. Med."},{"issue":"6","key":"10.1016\/j.bone.2020.115606_bb0680","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1242\/dev.072652","article-title":"SIK3 is essential for chondrocyte hypertrophy during skeletal development in mice","volume":"139","author":"Sasagawa","year":"2012","journal-title":"Development"},{"issue":"19","key":"10.1016\/j.bone.2020.115606_bb0685","doi-asserted-by":"crossref","first-page":"10240","DOI":"10.1073\/pnas.93.19.10240","article-title":"Targeted overexpression of parathyroid hormone-related peptide in chondrocytes causes chondrodysplasia and delayed endochondral bone formation","volume":"93","author":"Weir","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"459","key":"10.1016\/j.bone.2020.115606_bb0690","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.aat9356","article-title":"The PTH\/PTHrP-SIK3 pathway affects skeletogenesis through altered mTOR signaling","volume":"10","author":"Csukasi","year":"2018","journal-title":"Sci. Transl. Med."},{"issue":"12","key":"10.1016\/j.bone.2020.115606_bb0695","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1016\/j.tem.2018.09.007","article-title":"The salt-inducible kinases: emerging metabolic regulators","volume":"29","author":"Sakamoto","year":"2018","journal-title":"Trends Endocrinol. Metab."},{"issue":"10","key":"10.1016\/j.bone.2020.115606_bb0700","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1016\/j.tem.2018.08.004","article-title":"Salt-inducible kinases: physiology, regulation by cAMP, and therapeutic potential","volume":"29","author":"Wein","year":"2018","journal-title":"Trends Endocrinol Metab"},{"issue":"3","key":"10.1016\/j.bone.2020.115606_bb0705","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1111\/febs.14351","article-title":"14-3-3 Proteins mediate inhibitory effects of cAMP on salt-inducible kinases (SIKs)","volume":"285","author":"Sonntag","year":"2018","journal-title":"FEBS J."},{"issue":"1","key":"10.1016\/j.bone.2020.115606_bb0710","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1002\/jbm4.10021","article-title":"Parathyroid hormone signaling in osteocytes","volume":"2","author":"Wein","year":"2018","journal-title":"JBMR Plus"},{"issue":"12","key":"10.1016\/j.bone.2020.115606_bb0715","doi-asserted-by":"crossref","first-page":"5187","DOI":"10.1172\/JCI130126","article-title":"Salt-inducible kinases dictate parathyroid hormone 1 receptor action in bone development and remodeling","volume":"129","author":"Nishimori","year":"2019","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bone.2020.115606_bb0720","first-page":"688","article-title":"Cloning and characterization of four SIR genes of Saccharomyces cerevisiae","volume":"6","author":"Ivy","year":"1986","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bone.2020.115606_bb0725","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1124\/pr.110.003905","article-title":"Targeting sirtuin 1 to improve metabolism: all you need is NAD +?","volume":"64","author":"Cant\u00f3","year":"2012","journal-title":"Pharmacol. Rev."},{"key":"10.1016\/j.bone.2020.115606_bb0730","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1128\/JVI.03220-14","article-title":"Intricate roles of mammalian Sirtuins in defense against viral pathogens","volume":"90","author":"Budayeva","year":"2016","journal-title":"J. Virol."},{"key":"10.1016\/j.bone.2020.115606_bb0735","first-page":"53","article-title":"Transcription regulation by class III histone deacetylases (HDACs) - Sirtuins","volume":"2008","author":"Dai","year":"2008","journal-title":"Translational Oncogenomics"},{"key":"10.1016\/j.bone.2020.115606_bb0740","doi-asserted-by":"crossref","first-page":"3001","DOI":"10.1210\/en.2019-00427","article-title":"Cartilage ablation of Sirt1 causes inhibition of growth plate chondrogenesis by hyperactivation of mTORC1 signaling","volume":"160","author":"Jin","year":"2019","journal-title":"Endocrinology"},{"key":"10.1016\/j.bone.2020.115606_bb0745","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1002\/emmm.201201606","article-title":"SIRT1 regulates differentiation of mesenchymal stem cells by deacetylating \u03b2-catenin","volume":"5","author":"Simic","year":"2013","journal-title":"EMBO Molecular Medicine"},{"key":"10.1016\/j.bone.2020.115606_bb0750","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.metabol.2018.06.006","article-title":"Overexpression of Sirt1 in mesenchymal stem cells protects against bone loss in mice by FOXO3a deacetylation and oxidative stress inhibition","volume":"88","author":"Sun","year":"2018","journal-title":"Metabolism"},{"key":"10.1016\/j.bone.2020.115606_bb0755","doi-asserted-by":"crossref","DOI":"10.1038\/s41419-019-1569-2","article-title":"Nicotinamide mononucleotide promotes osteogenesis and reduces adipogenesis by regulating mesenchymal stromal cells via the SIRT1 pathway in aged bone marrow","volume":"10","author":"Song","year":"2019","journal-title":"Cell Death and Disease"},{"key":"10.1016\/j.bone.2020.115606_bb0760","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1007\/s10522-009-9221-7","article-title":"Effect of estrogens on bone marrow adipogenesis and Sirt1 in aging C57BL\/6J mice","volume":"10","author":"Elbaz","year":"2009","journal-title":"Biogerontology"},{"key":"10.1016\/j.bone.2020.115606_bb0765","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1359\/jbmr.060415","article-title":"Activation of Sirt1 decreases adipocyte formation during osteoblast differentiation of mesenchymal stem cells","volume":"21","author":"B\u00e4ckesj\u00f6","year":"2006","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bone.2020.115606_bb0770","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1159\/000151744","article-title":"Activation of Sirt1 decreases adipocyte formation during osteoblast differentiation of mesenchymal stem cells","volume":"189","author":"B\u00e4ckesj\u00f6","year":"2008","journal-title":"Cells Tissues Organs"},{"key":"10.1016\/j.bone.2020.115606_bb0775","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0035712","article-title":"Resveratrol mediated modulation of sirt-1\/Runx2 promotes osteogenic differentiation of mesenchymal stem cells: potential role of Runx2 deacetylation","volume":"7","author":"Shakibaei","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.bone.2020.115606_bb0780","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/j.bbrc.2016.06.154","article-title":"Sirtuin1 promotes osteogenic differentiation through downregulation of peroxisome proliferator-activated receptor \u03b3 in MC3T3-E1 cells","volume":"478","author":"Qu","year":"2016","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bone.2020.115606_bb0785","doi-asserted-by":"crossref","first-page":"393","DOI":"10.14348\/molcells.2017.0018","article-title":"Peroxisome proliferator-activated receptor \u03b1 facilitates osteogenic differentiation in MC3T3-E1 cells via the sirtuin 1-dependent signaling pathway","volume":"40","author":"Gong","year":"2017","journal-title":"Molecules and Cells"},{"key":"10.1016\/j.bone.2020.115606_bb0790","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.bbrc.2016.07.057","article-title":"MiR-132 regulates osteogenic differentiation via downregulating Sirtuin1 in a peroxisome proliferator-activated receptor \u03b2\/\u03b4\u2013dependent manner","volume":"478","author":"Gong","year":"2016","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bone.2020.115606_bb0795","doi-asserted-by":"crossref","first-page":"2552","DOI":"10.1002\/jbmr.460","article-title":"Resveratrol promotes osteogenesis of human mesenchymal stem cells by upregulating RUNX2 gene expression via the SIRT1\/FOXO3A axis","volume":"26","author":"Tseng","year":"2011","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bone.2020.115606_bb0800","first-page":"6681","article-title":"Upregulation of SIRT1 inhibits H2O2-induced osteoblast apoptosis eia FoxO1\/\u03b2-catenin pathway","volume":"17","author":"Yao","year":"2018","journal-title":"Mol. Med. Rep."},{"issue":"13","key":"10.1016\/j.bone.2020.115606_bb0805","doi-asserted-by":"crossref","first-page":"8373","DOI":"10.1074\/jbc.M114.602763","article-title":"Sirtuin 1 is a negative regulator of parathyroid hormone stimulation of matrix metalloproteinase 13 expression in osteoblastic cells: role of sirtuin 1 in the action of PTH on osteoblasts","volume":"290","author":"Fei","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bone.2020.115606_bb0810","doi-asserted-by":"crossref","first-page":"1130","DOI":"10.1002\/jcb.25070","article-title":"Resveratrol potentiates vitamin D and nuclear receptor signaling","volume":"116","author":"Dampf Stone","year":"2015","journal-title":"J. Cell. Biochem."},{"key":"10.1016\/j.bone.2020.115606_bb0815","doi-asserted-by":"crossref","first-page":"1917","DOI":"10.1007\/s00198-018-4547-0","article-title":"Vitamin D3 contributes to enhanced osteogenic differentiation of MSCs under oxidative stress condition via activating the endogenous antioxidant system","volume":"29","author":"Zhou","year":"2018","journal-title":"Osteoporos. Int."},{"key":"10.1016\/j.bone.2020.115606_bb0820","doi-asserted-by":"crossref","first-page":"4928","DOI":"10.1002\/jcb.26730","article-title":"Spontaneous up-regulation of SIRT1 during osteogenesis contributes to stem cells\u2019 resistance to oxidative stress","volume":"119","author":"Li","year":"2018","journal-title":"J. Cell. Biochem."},{"key":"10.1016\/j.bone.2020.115606_bb0825","doi-asserted-by":"crossref","first-page":"2969","DOI":"10.3892\/mmr.2017.6917","article-title":"Overexpression of SIRT1 prevents hypoxia-induced apoptosis in osteoblast cells","volume":"16","author":"Zhou","year":"2017","journal-title":"Mol. Med. Rep."},{"key":"10.1016\/j.bone.2020.115606_bb0830","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.freeradbiomed.2019.10.412","article-title":"Melatonin restores the osteoporosis-impaired osteogenic potential of bone marrow mesenchymal stem cells by preserving SIRT1-mediated intracellular antioxidant properties","volume":"146","author":"Chen","year":"2020","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.bone.2020.115606_bb0835","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1111\/jpi.12250","article-title":"Melatonin reverses H2O2-induced premature senescence in mesenchymal stem cells via the SIRT1-dependent pathway","volume":"59","author":"Zhou","year":"2015","journal-title":"J. Pineal Res."},{"key":"10.1016\/j.bone.2020.115606_bb0840","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1007\/s11357-012-9412-z","article-title":"Blueberry consumption prevents loss of collagen in bone matrix and inhibits senescence pathways in osteoblastic cells","volume":"35","author":"Zhang","year":"2013","journal-title":"Age"},{"key":"10.1016\/j.bone.2020.115606_bb0845","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1038\/aps.2011.189","article-title":"Sirt1 overexpression protects murine osteoblasts against TNF-\u03b1-induced injury in vitro by suppressing the NF-B signaling pathway","volume":"33","author":"Huang","year":"2012","journal-title":"Acta Pharmacol. Sin."},{"key":"10.1016\/j.bone.2020.115606_bb0850","doi-asserted-by":"crossref","first-page":"11492","DOI":"10.1074\/jbc.M110.198713","article-title":"Resveratrol-mediated SIRT-1 interactions with p300 modulate receptor activator of NF-\u03baB ligand (RANKL) activation of NF-\u03baB signaling and inhibit osteoclastogenesis in bone-derived cells","volume":"286","author":"Shakibaei","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bone.2020.115606_bb0855","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/20002297.2017.1317578","article-title":"Sirtuin 1 regulates matrix metalloproteinase-13 expression induced by Porphyromonas endodontalis lipopolysaccharide via targeting nuclear factor-B in osteoblasts","volume":"9","author":"Qu","year":"2017","journal-title":"Journal of Oral Microbiology"},{"key":"10.1016\/j.bone.2020.115606_bb0860","doi-asserted-by":"crossref","first-page":"1024","DOI":"10.1093\/abbs\/gmu103","article-title":"Protective effects of resveratrol on postmenopausal osteoporosis: regulation of SIRT1-NF-\u03baB signaling pathway","volume":"46","author":"Feng","year":"2014","journal-title":"Acta Biochim. Biophys. Sin."},{"key":"10.1016\/j.bone.2020.115606_bb0865","doi-asserted-by":"crossref","first-page":"3325","DOI":"10.1007\/s00198-017-4127-8","article-title":"Melatonin at pharmacological concentrations suppresses osteoclastogenesis via the attenuation of intracellular ROS","volume":"28","author":"Zhou","year":"2017","journal-title":"Osteoporos. Int."},{"key":"10.1016\/j.bone.2020.115606_bb0870","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1016\/j.bbrc.2010.09.053","article-title":"Resveratrol prevents RANKL-induced osteoclast differentiation of murine osteoclast progenitor RAW 264.7 cells through inhibition of ROS production","volume":"401","author":"He","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bone.2020.115606_bb0875","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1002\/cbf.3436","article-title":"MicroRNA-506 upregulation contributes to sirtuin 1 inhibition of osteoclastogenesis in bone marrow stromal cells induced by TNF-\u03b1 treatment","volume":"37","author":"Yan","year":"2019","journal-title":"Cell Biochem. Funct."},{"key":"10.1016\/j.bone.2020.115606_bb0880","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1016\/j.arcmed.2012.06.012","article-title":"Association study of Sirtuin 1 polymorphisms with bone mineral density and body mass index","volume":"43","author":"Zarrabeitia","year":"2012","journal-title":"Arch. Med. Res."},{"key":"10.1016\/j.bone.2020.115606_bb0885","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1111\/acel.12538","article-title":"Function of the SIRT3 mitochondrial deacetylase in cellular physiology, cancer, and neurodegenerative disease","volume":"16","author":"Ansari","year":"2017","journal-title":"Aging Cell"},{"key":"10.1016\/j.bone.2020.115606_bb0890","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fnagi.2013.00048","article-title":"Forever young: SIRT3 a shield against mitochondrial meltdown, aging, and neurodegeneration","volume":"5","author":"Kincaid","year":"2013","journal-title":"Front. Aging Neurosci."},{"key":"10.1016\/j.bone.2020.115606_bb0895","doi-asserted-by":"crossref","first-page":"254","DOI":"10.7150\/ijbs.17053","article-title":"Sirtuin 3 is required for osteogenic differentiation through maintenance of PGC-1\u0251-SOD2-mediated regulation of mitochondrial function","volume":"13","author":"Ding","year":"2017","journal-title":"Int. J. Biol. Sci."},{"key":"10.1016\/j.bone.2020.115606_bb0900","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1080\/15548627.2015.1052208","article-title":"SIRT3-SOD2-mROS-dependent autophagy in cadmium-induced hepatotoxicity and salvage by melatonin","volume":"11","author":"Pi","year":"2015","journal-title":"Autophagy"},{"key":"10.1016\/j.bone.2020.115606_bb0905","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/j.bbrc.2015.12.037","article-title":"Deacetylation of MnSOD by PARP-regulated SIRT3 protects retinal capillary endothelial cells from hyperglycemia-induced damage","volume":"472","author":"Gao","year":"2016","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bone.2020.115606_bb0910","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1152\/physrev.00022.2016","article-title":"Bone cell bioenergetics and skeletal energy homeostasis","volume":"97","author":"Riddle","year":"2017","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.bone.2020.115606_bb0915","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/srep22511","article-title":"Sirtuin 3 (SIRT3) maintains bone homeostasis by regulating AMPK-PGC-1\u03b2 axis in mice","volume":"6","author":"Huh","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bone.2020.115606_bb0920","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1038\/cdd.2017.144","article-title":"SIRT3\/SOD2 maintains osteoblast differentiation and bone formation by regulating mitochondrial stress","volume":"25","author":"Gao","year":"2018","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.bone.2020.115606_bb0925","first-page":"2095","article-title":"Zoledronic acid accelerates osteogenesis of bone marrow mesenchymal stem cells by attenuating oxidative stress via the SIRT3\/SOD2 pathway and thus alleviates osteoporosis","volume":"24","author":"Jin","year":"2020","journal-title":"Eur. Rev. Med. Pharmacol. Sci."},{"key":"10.1016\/j.bone.2020.115606_bb0930","doi-asserted-by":"crossref","DOI":"10.1155\/2019\/4019619","article-title":"Melatonin increases bone mass around the prostheses of OVX rats by ameliorating mitochondrial oxidative stress via the SIRT3\/SOD2 signaling pathway","volume":"2019","author":"Zhou","year":"2019","journal-title":"Oxidative Med. Cell. Longev."},{"key":"10.1016\/j.bone.2020.115606_bb0935","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1038\/nature10815","article-title":"The sirtuin SIRT6 regulates lifespan in male mice","volume":"483","author":"Kanfi","year":"2012","journal-title":"Nature"},{"key":"10.1016\/j.bone.2020.115606_bb0940","doi-asserted-by":"crossref","DOI":"10.3390\/biom8030044","article-title":"A review of the recent advances made with SIRT6 and its implications on aging related processes, major human diseases, and possible therapeutic targets","volume":"8","author":"Khan","year":"2018","journal-title":"Biomolecules"},{"key":"10.1016\/j.bone.2020.115606_bb0945","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/j.cell.2005.11.044","article-title":"Genomic instability and aging-like phenotype in the absence of mammalian SIRT6","volume":"124","author":"Mostoslavsky","year":"2006","journal-title":"Cell"},{"key":"10.1016\/j.bone.2020.115606_bb0950","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/srep03022","article-title":"Sirt6 regulates postnatal growth plate differentiation and proliferation via Ihh signaling","volume":"3","author":"Piao","year":"2013","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bone.2020.115606_bb0955","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1038\/ijos.2015.57","article-title":"Phenotypic research on senile osteoporosis caused by SIRT6 deficiency","volume":"8","author":"Zhang","year":"2016","journal-title":"International Journal of Oral Science"},{"key":"10.1016\/j.bone.2020.115606_bb0960","doi-asserted-by":"crossref","first-page":"8412","DOI":"10.12659\/MSM.917118","article-title":"Inhibitory effect of Sirtuin6 (SIRT6) on osteogenic differentiation of bone marrow mesenchymal stem cells","volume":"25","author":"Xiao","year":"2019","journal-title":"Med. Sci. Monit."},{"key":"10.1016\/j.bone.2020.115606_bb0965","doi-asserted-by":"crossref","first-page":"1943","DOI":"10.1002\/stem.1671","article-title":"SIRT6 regulates osteogenic differentiation of rat bone marrow mesenchymal stem cells partially via suppressing the nuclear factor-\u03baB signaling pathway","volume":"32","author":"Sun","year":"2014","journal-title":"Stem Cells"},{"key":"10.1016\/j.bone.2020.115606_bb0970","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1016\/j.phrs.2017.11.020","article-title":"Metformin promotes the proliferation and differentiation of murine preosteoblast by regulating the expression of sirt6 and oct4","volume":"129","author":"Mu","year":"2018","journal-title":"Pharmacol. Res."},{"issue":"5","key":"10.1016\/j.bone.2020.115606_bb0975","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1016\/j.stem.2013.10.010","article-title":"Deciphering hematopoietic stem cells in their niches: a critical appraisal of genetic models, lineage tracing, and imaging strategies","volume":"13","author":"Joseph","year":"2013","journal-title":"Cell Stem Cell"},{"key":"10.1016\/j.bone.2020.115606_bb0980","first-page":"1","article-title":"Sirt6 cooperates with Blimp1 to positively regulate osteoclast differentiation","volume":"6","author":"Park","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bone.2020.115606_bb0985","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fendo.2018.00652","article-title":"Advances in cellular characterization of the sirtuin isoform, SIRT7","volume":"9","author":"Wu","year":"2018","journal-title":"Front. Endocrinol."},{"key":"10.1016\/j.bone.2020.115606_bb0990","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-018-05187-4","article-title":"SIRT7 has a critical role in bone formation by regulating lysine acylation of SP7\/Osterix","volume":"9","author":"Fukuda","year":"2018","journal-title":"Nat. Commun."}],"container-title":["Bone"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S8756328220303860?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S8756328220303860?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,16]],"date-time":"2026-05-16T14:13:59Z","timestamp":1778940839000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S8756328220303860"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,2]]},"references-count":198,"alternative-id":["S8756328220303860"],"URL":"https:\/\/doi.org\/10.1016\/j.bone.2020.115606","relation":{},"ISSN":["8756-3282"],"issn-type":[{"value":"8756-3282","type":"print"}],"subject":[],"published":{"date-parts":[[2021,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Role of histone deacetylases in bone development and skeletal disorders","name":"articletitle","label":"Article Title"},{"value":"Bone","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bone.2020.115606","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"115606"}}