{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T21:57:29Z","timestamp":1792706249792,"version":"4.5.0"},"reference-count":137,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2022,4,20]],"date-time":"2022-04-20T00:00:00Z","timestamp":1650412800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Mitochondria play a crucial role in cell physiology and pathophysiology. In this context, mitochondrial dynamics and, subsequently, mitochondrial ultrastructure have increasingly become hot topics in modern research, with a focus on mitochondrial fission and fusion. Thus, the dynamics of mitochondria in several diseases have been intensively investigated, especially with a view to developing new promising treatment options. However, the majority of recent studies are performed in highly energy-dependent tissues, such as cardiac, hepatic, and neuronal tissues. In contrast, publications on mitochondrial dynamics from the orthopedic or trauma fields are quite rare, even if there are common cellular mechanisms in cardiovascular and bone tissue, especially regarding bone infection. The present report summarizes the spectrum of mitochondrial alterations in the cardiovascular system and compares it to the state of knowledge in the musculoskeletal system. The present paper summarizes recent knowledge regarding mitochondrial dynamics and gives a short, but not exhaustive, overview of its regulation via fission and fusion. Furthermore, the article highlights hypoxia and its accompanying increased mitochondrial fission as a possible link between cardiac ischemia and inflammatory diseases of the bone, such as osteomyelitis. This opens new innovative perspectives not only for the understanding of cellular pathomechanisms in osteomyelitis but also for potential new treatment options.<\/jats:p>","DOI":"10.3390\/ijms23094571","type":"journal-article","created":{"date-parts":[[2022,4,21]],"date-time":"2022-04-21T01:55:51Z","timestamp":1650506151000},"page":"4571","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":20,"title":["Structural Analysis of Mitochondrial Dynamics\u2014From Cardiomyocytes to Osteoblasts: A Critical Review"],"prefix":"10.3390","volume":"23","author":[{"given":"Daniel H.","family":"Mendelsohn","sequence":"first","affiliation":[{"name":"Institute of Pathology, University Regensburg, 93053 Regensburg, Germany"},{"name":"Central Biobank Regensburg, University Regensburg, University Hospital Regensburg, 93053 Regensburg, Germany"},{"name":"Department of Trauma Surgery, University Medical Centre Regensburg, 93053 Regensburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katja","family":"Schnabel","sequence":"additional","affiliation":[{"name":"Institute of Pathology, University Regensburg, 93053 Regensburg, Germany"},{"name":"Central Biobank Regensburg, University Regensburg, University Hospital Regensburg, 93053 Regensburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0895-5675","authenticated-orcid":false,"given":"Andreas","family":"Mamilos","sequence":"additional","affiliation":[{"name":"Institute of Pathology, University Regensburg, 93053 Regensburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8034-2673","authenticated-orcid":false,"given":"Samuel","family":"Sossalla","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine II, University Hospital Regensburg, 93053 Regensburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steffen","family":"Pabel","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine II, University Hospital Regensburg, 93053 Regensburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0310-6236","authenticated-orcid":false,"given":"Georg Daniel","family":"Duerr","sequence":"additional","affiliation":[{"name":"Department of Cardiovascular Surgery, University Medical Center Mainz (Johannes Gutenberg-University Mainz), 55131 Mainz, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0820-9584","authenticated-orcid":false,"given":"Karsten","family":"Keller","sequence":"additional","affiliation":[{"name":"Department of Cardiology, Cardiology I, University Medical Center Mainz (Johannes Gutenberg-University Mainz), 55131 Mainz, Germany"},{"name":"Center for Thrombosis and Hemostasis (CTH), University Medical Center Mainz (Johannes Gutenberg-University Mainz), 55131 Mainz, Germany"},{"name":"Department of Sports Medicine, Medical Clinic VII, University Hospital Heidelberg, 69120 Heidelberg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5070-7280","authenticated-orcid":false,"given":"Volker H.","family":"Schmitt","sequence":"additional","affiliation":[{"name":"Department of Cardiology, Cardiology I, University Medical Center Mainz (Johannes Gutenberg-University Mainz), 55131 Mainz, Germany"},{"name":"German Center for Cardiovascular Research (DZHK), Partner Site Rhine Main, 55131 Mainz, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6189-7259","authenticated-orcid":false,"given":"Friedrich","family":"Barsch","sequence":"additional","affiliation":[{"name":"Institute for Exercise and Occupational Medicine, Faculty of Medicine, Medical Center, University of Freiburg, 79106 Freiburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0654-2076","authenticated-orcid":false,"given":"Nike","family":"Walter","sequence":"additional","affiliation":[{"name":"Department of Trauma Surgery, University Medical Centre Regensburg, 93053 Regensburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ronald Man Yeung","family":"Wong","sequence":"additional","affiliation":[{"name":"Department of Orthopaedics and Traumatology, Prince of Wales Hospital, The Chinese University of Hong Kong, Hong Kong, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1187-8578","authenticated-orcid":false,"given":"Thaqif","family":"El Khassawna","sequence":"additional","affiliation":[{"name":"Department of Experimental Trauma Surgery, Justus-Liebig-University Giessen, 35390 Giessen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tanja","family":"Niedermair","sequence":"additional","affiliation":[{"name":"Institute of Pathology, University Regensburg, 93053 Regensburg, Germany"},{"name":"Central Biobank Regensburg, University Regensburg, University Hospital Regensburg, 93053 Regensburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0208-4650","authenticated-orcid":false,"given":"Volker","family":"Alt","sequence":"additional","affiliation":[{"name":"Department of Trauma Surgery, University Medical Centre Regensburg, 93053 Regensburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7221-3783","authenticated-orcid":false,"given":"Markus","family":"Rupp","sequence":"additional","affiliation":[{"name":"Department of Trauma Surgery, University Medical Centre Regensburg, 93053 Regensburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6761-0247","authenticated-orcid":false,"given":"Christoph","family":"Brochhausen","sequence":"additional","affiliation":[{"name":"Institute of Pathology, University Regensburg, 93053 Regensburg, Germany"},{"name":"Central Biobank Regensburg, University Regensburg, University Hospital Regensburg, 93053 Regensburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,4,20]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Annesley, S.J., and Fisher, P.R. (2019). Mitochondria in health and disease. Cells, 8.","DOI":"10.3390\/cells8070680"},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Protasoni, M., and Zeviani, M. (2021). Mitochondrial structure and bioenergetics in normal and disease conditions. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22020586"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1146\/annurev-pathmechdis-012419-032711","article-title":"Mitochondrial Dynamics and Its Involvement in Disease","volume":"15","author":"Chan","year":"2020","journal-title":"Annu. Rev. Pathol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1038\/nm.2282","article-title":"miR-499 regulates mitochondrial dynamics by targeting calcineurin and dynamin-related protein-1","volume":"17","author":"Wang","year":"2011","journal-title":"Nat. Med."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1007\/s00018-017-2603-0","article-title":"The ever-growing complexity of the mitochondrial fission machinery","volume":"75","author":"Pagliuso","year":"2018","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"858","DOI":"10.1126\/science.1099793","article-title":"Structural basis of mitochondrial tethering by mitofusin complexes","volume":"305","author":"Koshiba","year":"2004","journal-title":"Science"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1016\/j.cmet.2014.03.011","article-title":"Proteolytic cleavage of Opa1 stimulates mitochondrial inner membrane fusion and couples fusion to oxidative phosphorylation","volume":"19","author":"Mishra","year":"2014","journal-title":"Cell Metab."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"624","DOI":"10.1016\/j.ijid.2020.12.047","article-title":"Secondary hemophagocytic lymphohistiocytosis and severe liver injury induced by hepatic SARS-CoV-2 infection unmasking Wilson\u2019s disease: Balancing immunosuppression","volume":"103","author":"Lubnow","year":"2021","journal-title":"Int. J. Infect. Dis."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"3006","DOI":"10.1038\/s41467-021-23334-2","article-title":"Severe T cell hyporeactivity in ventilated COVID-19 patients correlates with prolonged virus persistence and poor outcomes","volume":"12","author":"Renner","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"e148225","DOI":"10.1172\/JCI148225","article-title":"Metabolic imbalance of T cells in COVID-19 is hallmarked by basigin and mitigated by dexamethasone","volume":"131","author":"Siska","year":"2021","journal-title":"J. Clin. Investig."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"e003872","DOI":"10.1161\/JAHA.116.003872","article-title":"Nanoparticle-mediated delivery of mitochondrial division inhibitor 1 to the myocardium protects the heart from ischemia-reperfusion injury through inhibition of mitochondria outer membrane permeabilization: A new therapeutic modality for acute myocardial infarction","volume":"5","author":"Ishikita","year":"2016","journal-title":"J. Am. Heart Assoc."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1096\/fj.12-226225","article-title":"Dynamin-related protein 1 (Drp1)-mediated diastolic dysfunction in myocardial ischemia-reperfusion injury: Therapeutic benefits of Drp1 inhibition to reduce mitochondrial fission","volume":"28","author":"Sharp","year":"2014","journal-title":"FASEB J."},{"key":"ref_13","unstructured":"Morio, B., P\u00e9nicaud, L., and Rigoulet, M. (2019). Chapter 1\u2014Mitochondria: Ultrastructure, dynamics, biogenesis and main functions. Mitochondria in Obesity and Type 2 Diabetes, Academic Press."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"K\u00fchlbrandt, W. (2015). Structure and function of mitochondrial membrane protein complexes. BMC Biol., 13.","DOI":"10.1186\/s12915-015-0201-x"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"30610","DOI":"10.1038\/srep30610","article-title":"The Spectrum of Mitochondrial Ultrastructural Defects in Mitochondrial Myopathy","volume":"6","author":"Vincent","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"e29929","DOI":"10.7554\/eLife.29929","article-title":"3D visualization of mitochondrial solid-phase calcium stores in whole cells","volume":"6","author":"Wolf","year":"2017","journal-title":"eLife"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/j.tibs.2016.01.001","article-title":"Mitochondrial cristae: Where beauty meets functionality","volume":"41","author":"Cogliati","year":"2016","journal-title":"Trends Biochem. Sci."},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Kondadi, A.K., Anand, R., and Reichert, A.S. (2019). Functional interplay between cristae biogenesis, mitochondrial dynamics and mitochondrial DNA integrity. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20174311"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"2779","DOI":"10.1113\/JP274158","article-title":"Mitochondrial cristae density: A dynamic entity that is critical for energy production and metabolic power in skeletal muscle","volume":"595","author":"Leveille","year":"2017","journal-title":"J. Physiol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"4706","DOI":"10.1038\/sj.onc.1209600","article-title":"Mitochondria and cancer: Is there a morphological connection?","volume":"25","author":"Alirol","year":"2006","journal-title":"Oncogene"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"292","DOI":"10.3389\/fonc.2013.00292","article-title":"Mitochondrial dysfunction in cancer","volume":"3","author":"Boland","year":"2013","journal-title":"Front. Oncol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/S1567-7249(01)00038-1","article-title":"Lamellar and tubular associations of the mitochondrial cristae: Unique forms of the cristae present in steroid-producing cells","volume":"1","author":"Prince","year":"2002","journal-title":"Mitochondrion"},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Chaanine, A.H. (2019). Morphological stages of mitochondrial vacuolar degeneration in phenylephrine-stressed cardiac myocytes and in animal models and human heart failure. Medicina, 55.","DOI":"10.3390\/medicina55060239"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"670267","DOI":"10.3389\/fragi.2021.670267","article-title":"Mitochondrial morphology and mitophagy in heart diseases: Qualitative and quantitative analyses using transmission electron microscopy","volume":"2","author":"Collins","year":"2021","journal-title":"Front. Aging"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1161\/CIR.0b013e3181d22e2d","article-title":"Giant mitochondria in the myocardium of a patient with mitochondrial cardiomyopathy","volume":"121","author":"Kanzaki","year":"2010","journal-title":"Circulation"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Ma, X., McKeen, T., Zhang, J., and Ding, W.-X. (2020). Role and mechanisms of mitophagy in liver diseases. Cells, 9.","DOI":"10.3390\/cells9040837"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"E2174","DOI":"10.1073\/pnas.1504880112","article-title":"Mitofusin 2 ablation increases endoplasmic reticulum\u2013mitochondria coupling","volume":"112","author":"Filadi","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1992","DOI":"10.3389\/fmicb.2020.01992","article-title":"Mitochondrial dynamics imbalance: A strategy for promoting viral infection","volume":"11","author":"Ren","year":"2020","journal-title":"Front. Microbiol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"6569728","DOI":"10.1155\/2020\/6569728","article-title":"Hyperglycemia induces endoplasmic reticulum stress in atrial cardiomyocytes, and mitofusin-2 downregulation prevents mitochondrial dysfunction and subsequent cell death","volume":"2020","author":"Yuan","year":"2020","journal-title":"Oxid. Med. Cell. Longev."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"e201911122","DOI":"10.1083\/jcb.201911122","article-title":"Fission and fusion machineries converge at ER contact sites to regulate mitochondrial morphology","volume":"219","author":"Abrisch","year":"2020","journal-title":"J. Cell Biol."},{"key":"ref_31","unstructured":"Ghadially, F.N. (1988). Ultrastructural Pathology of the Cell and Matrix, Butterworth-Heinemann. [3rd ed.]."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Tandler, B., Hoppel, C., and Mears, J. (2018). Morphological pathways of mitochondrial division. Antioxidants, 7.","DOI":"10.3390\/antiox7020030"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1455","DOI":"10.1002\/ar.22523","article-title":"Mitochondrial division in rat cardiomyocytes: An electron microscope study","volume":"295","author":"Fujioka","year":"2012","journal-title":"Anat. Rec."},{"key":"ref_34","first-page":"69","article-title":"Riboflavin and mouse hepatic cell structure and function. I. Ultrastructural alterations in simple deficiency","volume":"52","author":"Tandler","year":"1968","journal-title":"Am. J. Pathol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/0014-4800(74)90081-1","article-title":"Ultrastructural effects of dietary galactoflavin on mouse hepatocytes","volume":"21","author":"Tandler","year":"1974","journal-title":"Exp. Mol. Pathol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"2846","DOI":"10.1073\/pnas.1300741110","article-title":"Kissing and nanotunneling mediate intermitochondrial communication in the heart","volume":"110","author":"Huang","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"3074","DOI":"10.1038\/emboj.2009.255","article-title":"Mitochondrial \u2019kiss-and-run\u2019: Interplay between mitochondrial motility and fusion-fission dynamics","volume":"28","author":"Liu","year":"2009","journal-title":"EMBO J."},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Van der Bliek, A.M., Shen, Q., and Kawajiri, S. (2013). Mechanisms of mitochondrial fission and fusion. Cold Spring Harb. Perspect. Biol., 5.","DOI":"10.1101\/cshperspect.a011072"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.mito.2019.11.006","article-title":"OPA1 regulates respiratory supercomplexes assembly: The role of mitochondrial swelling","volume":"51","author":"Jang","year":"2020","journal-title":"Mitochondrion"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1042\/EBC20170104","article-title":"Mitochondrial dynamics: Overview of molecular mechanisms","volume":"62","author":"Tilokani","year":"2018","journal-title":"Essays Biochem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1091\/mbc.e12-10-0721","article-title":"Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission","volume":"24","author":"Song","year":"2013","journal-title":"Mol. Biol. Cell"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1849","DOI":"10.1080\/21505594.2016.1276690","article-title":"Altered mitochondrial dynamics as a consequence of Venezuelan Equine encephalitis virus infection","volume":"8","author":"Keck","year":"2017","journal-title":"Virulence"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1016\/j.fsi.2018.07.003","article-title":"Preliminary investigations on the role of Drp-1 dependent mitochondrial fission in attenuating RLR downstream signaling during nervous necrosis virus infection","volume":"80","author":"Krishnan","year":"2018","journal-title":"Fish Shellfish. Immunol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1016\/j.cell.2014.10.023","article-title":"ER contact sites define the position and timing of endosome fission","volume":"159","author":"Rowland","year":"2014","journal-title":"Cell"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1126\/science.1207385","article-title":"ER tubules mark sites of mitochondrial division","volume":"334","author":"Friedman","year":"2011","journal-title":"Science"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1083\/jcb.200903065","article-title":"The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice","volume":"186","author":"Wakabayashi","year":"2009","journal-title":"J. Cell Biol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"121523","DOI":"10.1016\/j.talanta.2020.121523","article-title":"Rapid and quantitative in vitro analysis of mitochondrial fusion and its interplay with apoptosis","volume":"222","author":"Xu","year":"2021","journal-title":"Talanta"},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Gupte, T.M. (2015). Mitochondrial fragmentation due to inhibition of fusion increases cyclin B through mitochondrial superoxide radicals. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0126829"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1804","DOI":"10.1038\/s41418-020-00705-8","article-title":"ER-mitochondria contact sites in neurodegeneration: Genetic screening approaches to investigate novel disease mechanisms","volume":"28","author":"Wilson","year":"2021","journal-title":"Cell Death Differ."},{"key":"ref_50","unstructured":"Alberts, B., Johnson, A., Lewis, J., Raff, M., Roberts, K., and Walter, P. (2002). Molecular Biology of the Cell, Garland Science. [4th ed.]."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1042\/bj1190157","article-title":"Haem a, cytochrome c and total protein turnover in mitochondria from rat heart and liver","volume":"119","author":"Aschenbrenner","year":"1970","journal-title":"Biochem. J."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1083\/jcb.48.1.29","article-title":"Control of mitochondrial turnover under the influence of thyroid hormone","volume":"48","author":"Gross","year":"1971","journal-title":"J. Cell Biol."},{"key":"ref_53","unstructured":"Serov, V.V. (2010). Strukov. Pathological Anatomy a Textbook\/Patologicheskaya Anatomiya Uchebnik, Litterra."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"e71","DOI":"10.15190\/d.2017.1","article-title":"Unique morphological characteristics of mitochondrial subtypes in the heart: The effect of ischemia and ischemic preconditioning","volume":"5","author":"Kalkhoran","year":"2017","journal-title":"Discoveries"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1975","DOI":"10.1016\/j.freeradbiomed.2011.08.022","article-title":"Novel insights into interactions between mitochondria and xanthine oxidase in acute cardiac volume overload","volume":"51","author":"Gladden","year":"2011","journal-title":"Free Radic. Biol. Med."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/j.yjmcc.2010.10.034","article-title":"Loss of interstitial collagen causes structural and functional alterations of cardiomyocyte subsarcolemmal mitochondria in acute volume overload","volume":"50","author":"Ulasova","year":"2011","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Poznyak, A.V., Ivanova, E.A., Sobenin, I.A., Yet, S.-F., and Orekhov, A.N. (2020). The role of mitochondria in cardiovascular diseases. Biology, 9.","DOI":"10.3390\/biology9060137"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"e005131","DOI":"10.1161\/CIRCHEARTFAILURE.118.005131","article-title":"Mitochondrial morphology, dynamics, and function in human pressure overload or ischemic heart disease with preserved or reduced ejection fraction","volume":"12","author":"Chaanine","year":"2019","journal-title":"Circ. Heart Fail."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1096\/fj.04-2622fje","article-title":"Age-associated increases in oxidative stress and antioxidant enzyme activities in cardiac interfibrillar mitochondria: Implications for the mitochondrial theory of aging","volume":"19","author":"Judge","year":"2005","journal-title":"FASEB J."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1395","DOI":"10.1161\/CIRCRESAHA.112.270801","article-title":"Novel role for the regulation of mitochondrial fission by HIF-1\u03b1 in the control of smooth muscle remodeling and progression of pulmonary hypertension","volume":"110","author":"Wolin","year":"2012","journal-title":"Circ. Res."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1146\/annurev-physiol-021113-170322","article-title":"Hypoxia-inducible factor 1 and cardiovascular disease","volume":"76","author":"Semenza","year":"2014","journal-title":"Annu. Rev. Physiol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1038\/labinvest.2010.43","article-title":"Impairment of ultrastructure and cytoskeleton during progression of cardiac hypertrophy to heart failure","volume":"90","author":"Gupta","year":"2010","journal-title":"Lab. Investig. A J. Tech. Methods Pathol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1093\/cvr\/28.1.1","article-title":"Mitochondrial function in the oxygen depleted and reoxygenated myocardial cell","volume":"28","author":"Piper","year":"1994","journal-title":"Cardiovasc. Res."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1134\/S1990519X17060086","article-title":"The features of mitochondria of cardiomyocytes from rats with chronic heart failure","volume":"11","author":"Stepanov","year":"2017","journal-title":"Cell Tissue Biol."},{"key":"ref_65","unstructured":"Lennarz, W.J., and Lane, M.D. (2013). Giant mitochondria (megamitochondria). Encyclopedia of Biological Chemistry, Academic Press. [2nd ed.]."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1949","DOI":"10.1016\/j.biocel.2009.05.004","article-title":"Dynamic organization of mitochondria in human heart and in myocardial disease","volume":"41","author":"Hoppel","year":"2009","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_67","unstructured":"Tondera, D. (2021, June 04). SLP-2 Is Required for Stress-Induced Mitochondrial Hyperfusion\u2014PubMed, Available online: https:\/\/pubmed.ncbi.nlm.nih.gov\/19360003\/."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1111\/j.1582-4934.2002.tb00452.x","article-title":"Megamitochondria formation\u2014physiology and pathology","volume":"6","author":"Wakabayashi","year":"2002","journal-title":"J. Cell. Mol. Med."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1007\/s00395-012-0268-2","article-title":"Metabolic adaptation to chronic hypoxia in cardiac mitochondria","volume":"107","author":"Heather","year":"2012","journal-title":"Basic Res. Cardiol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1161\/CIRCULATIONAHA.119.040551","article-title":"Unlocking the secrets of mitochondria in the cardiovascular system: Path to a cure in heart failure\u2014A report from the 2018 national heart, lung, and blood institute workshop","volume":"140","author":"Tian","year":"2019","journal-title":"Circulation"},{"key":"ref_71","first-page":"935","article-title":"Targeting reperfusion injury in patients with ST-segment elevation myocardial infarction: Trials and tribulations","volume":"38","author":"Hausenloy","year":"2017","journal-title":"Eur. Heart J."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1161\/CIRCRESAHA.116.303356","article-title":"Endogenous Drp1 mediates mitochondrial autophagy and protects the heart against energy stress","volume":"116","author":"Ikeda","year":"2015","journal-title":"Circ. Res."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"6571","DOI":"10.1111\/jcmm.15384","article-title":"Targeting mitochondrial fusion and fission proteins for cardioprotection","volume":"24","author":"Prunier","year":"2020","journal-title":"J. Cell. Mol. Med."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1111\/apha.12812","article-title":"High glucose concentration abrogates sevoflurane post-conditioning cardioprotection by advancing mitochondrial fission but dynamin-related protein 1 inhibitor restores these effects","volume":"220","author":"Yu","year":"2017","journal-title":"Acta Physiol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1447","DOI":"10.1096\/fj.201901467R","article-title":"Identification of novel dynamin-related protein 1 (Drp1) GTPase inhibitors: Therapeutic potential of Drpitor1 and Drpitor1a in cancer and cardiac ischemia-reperfusion injury","volume":"34","author":"Wu","year":"2020","journal-title":"FASEB J."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"583\u2013594.e6","DOI":"10.1016\/j.devcel.2017.02.020","article-title":"The putative Drp1 inhibitor mdivi-1 is a reversible mitochondrial complex I inhibitor that modulates reactive oxygen species","volume":"40","author":"Bordt","year":"2017","journal-title":"Dev. Cell"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1097\/FJC.0000000000000071","article-title":"Drp1 loss-of-function reduces cardiomyocyte oxygen dependence protecting the heart from ischemia-reperfusion injury","volume":"63","author":"Zepeda","year":"2014","journal-title":"J. Cardiovasc. Pharmacol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"e000461","DOI":"10.1161\/JAHA.113.000461","article-title":"Acute inhibition of excessive mitochondrial fission after myocardial infarction prevents long-term cardiac dysfunction","volume":"2","author":"Disatnik","year":"2013","journal-title":"J. Am. Heart Assoc."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"e12413","DOI":"10.1111\/jpi.12413","article-title":"Melatonin protects cardiac microvasculature against ischemia\/reperfusion injury via suppression of mitochondrial fission-VDAC1-HK2-mPTP-mitophagy axis","volume":"63","author":"Zhou","year":"2017","journal-title":"J. Pineal Res."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1007\/s10456-018-9611-z","article-title":"BI1 is associated with microvascular protection in cardiac ischemia reperfusion injury via repressing Syk-Nox2-Drp1-mitochondrial fission pathways","volume":"21","author":"Zhou","year":"2018","journal-title":"Angiogenesis"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/j.redox.2017.12.019","article-title":"Empagliflozin rescues diabetic myocardial microvascular injury via AMPK-mediated inhibition of mitochondrial fission","volume":"15","author":"Zhou","year":"2018","journal-title":"Redox Biol."},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Je\u017eek, J., Cooper, K., and Strich, R. (2018). Reactive oxygen species and mitochondrial dynamics: The Yin and Yang of mitochondrial dysfunction and cancer progression. Antioxidants, 7.","DOI":"10.3390\/antiox7010013"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"165728","DOI":"10.1016\/j.bbadis.2020.165728","article-title":"Regulation of metabolism by mitochondrial enzyme acetylation in cardiac ischemia-reperfusion injury","volume":"1866","author":"Herr","year":"2020","journal-title":"Biochim. Biophys. Acta (BBA)\u2014Mol. Basis Dis."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.freeradbiomed.2014.03.011","article-title":"Acute hypoxia produces a superoxide burst in cells","volume":"71","author":"Ramos","year":"2014","journal-title":"Free Radic. Biol. Med."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1038\/nature13909","article-title":"Ischaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS","volume":"515","author":"Chouchani","year":"2014","journal-title":"Nature"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1007\/s00223-021-00828-1","article-title":"Mitochondria homeostasis and vascular medial calcification","volume":"109","author":"Li","year":"2021","journal-title":"Calcif. Tissue Int."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1903","DOI":"10.1007\/s10439-012-0568-6","article-title":"Mitochondrial dynamics and motility inside living vascular endothelial cells: Role of bioenergetics","volume":"40","author":"Giedt","year":"2012","journal-title":"Ann. Biomed. Eng."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1007\/s10456-020-09720-2","article-title":"New insights into the role of mitochondria in cardiac microvascular ischemia\/reperfusion injury","volume":"23","author":"Wang","year":"2020","journal-title":"Angiogenesis"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1080\/03008207.2017.1290085","article-title":"Osteoblast-osteoclast interactions","volume":"59","author":"Chen","year":"2018","journal-title":"Connect. Tissue Res."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1016\/j.ecl.2015.05.002","article-title":"Bone Health and Osteoporosis","volume":"44","author":"Lupsa","year":"2015","journal-title":"Endocrinol. Metab. Clin. N. Am."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1210\/er.2009-0024","article-title":"From estrogen-centric to aging and oxidative stress: A revised perspective of the pathogenesis of osteoporosis","volume":"31","author":"Manolagas","year":"2010","journal-title":"Endocr. Rev."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1038\/nature01660","article-title":"Control of osteoblast function and regulation of bone mass","volume":"423","author":"Harada","year":"2003","journal-title":"Nature"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"2030","DOI":"10.1210\/me.2010-0189","article-title":"Oxidative stress stimulates apoptosis and activates NF-kappaB in osteoblastic cells via a PKCbeta\/p66shc signaling cascade: Counter regulation by estrogens or androgens","volume":"24","author":"Almeida","year":"2010","journal-title":"Mol. Endocrinol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1002\/ar.20925","article-title":"Hydrogen peroxide induces G2 cell cycle arrest and inhibits cell proliferation in osteoblasts","volume":"292","author":"Li","year":"2009","journal-title":"Anat. Rec."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1016\/S0891-5849(01)00610-4","article-title":"Oxidative stress modulates osteoblastic differentiation of vascular and bone cells","volume":"31","author":"Mody","year":"2001","journal-title":"Free Radic. Biol. Med."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1646","DOI":"10.1016\/j.freeradbiomed.2010.08.024","article-title":"H2O2-induced mitochondrial fragmentation in C2C12 myocytes","volume":"49","author":"Fan","year":"2010","journal-title":"Free Radic. Biol. Med."},{"key":"ref_97","doi-asserted-by":"crossref","unstructured":"Je\u017eek, J., Cooper, K.F., and Strich, R. (2021). The impact of mitochondrial fission-stimulated ROS production on pro-apoptotic chemotherapy. Biology, 10.","DOI":"10.3390\/biology10010033"},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"Vermot, A., Petit-H\u00e4rtlein, I., Smith, S.M.E., and Fieschi, F. (2021). NADPH oxidases (NOX): An overview from discovery, molecular mechanisms to physiology and pathology. Antioxidants, 10.","DOI":"10.3390\/antiox10060890"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1016\/j.bbrc.2015.11.022","article-title":"Blockade of Drp1 rescues oxidative stress-induced osteoblast dysfunction","volume":"468","author":"Gan","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1007\/s11914-015-0260-5","article-title":"Diabetes, diabetic complications, and fracture risk","volume":"13","author":"Oei","year":"2015","journal-title":"Curr. Osteoporos. Rep."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1007\/s11010-020-03732-8","article-title":"Hyperglycemia impairs osteoblast cell migration and chemotaxis due to a decrease in mitochondrial biogenesis","volume":"469","author":"Pahwa","year":"2020","journal-title":"Mol. Cell. Biochem."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1016\/j.devcel.2013.02.010","article-title":"Dynamin 2 potentiates invasive migration of pancreatic tumor cells through stabilization of the Rac1 GEF Vav1","volume":"24","author":"Razidlo","year":"2013","journal-title":"Dev. Cell"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1111\/brv.12345","article-title":"Osteoblast migration in vertebrate bone","volume":"93","author":"Thiel","year":"2018","journal-title":"Biol. Rev. Camb. Philos. Soc."},{"key":"ref_104","unstructured":"Rupp, M., Alt, V., and Lowenberg, D. (2022). Management of acute and chronic osteomyelitis. Orthopaedic Knowledge Update: Trauma 6, Wolters Kluwer. [6th ed.]."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.idc.2017.01.010","article-title":"Osteomyelitis","volume":"31","author":"Schmitt","year":"2017","journal-title":"Infect. Dis. Clin. N. Am."},{"key":"ref_106","doi-asserted-by":"crossref","unstructured":"Walter, N., Mendelsohn, D., Brochhausen, C., Rupp, M., and Alt, V. (2021). Intracellular S. aureus in osteoblasts in a clinical sample from a patient with chronic osteomyelitis\u2014A case report. Pathogens, 10.","DOI":"10.3390\/pathogens10081064"},{"key":"ref_107","unstructured":"Momodu, I.I., and Savaliya, V. (2021). Osteomyelitis. StatPearls, StatPearls Publishing."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"985","DOI":"10.1002\/jbmr.3055","article-title":"Evidence of staphylococcus aureus deformation, proliferation, and migration in canaliculi of live cortical bone in murine models of osteomyelitis: S. aureus in canaliculi of cortical bone in murine models of osteomyelitis","volume":"32","author":"Trombetta","year":"2017","journal-title":"J. Bone Miner. Res."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.7150\/ijms.45960","article-title":"The process of osteoblastic infection by staphylococcus aureus","volume":"17","author":"Wen","year":"2020","journal-title":"Int. J. Med. Sci."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"42","DOI":"10.3389\/fcimb.2019.00042","article-title":"How viral and intracellular bacterial pathogens reprogram the metabolism of host cells to allow their intracellular replication","volume":"9","author":"Eisenreich","year":"2019","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"615450","DOI":"10.3389\/fcimb.2020.615450","article-title":"Persistence of intracellular bacterial pathogens\u2014With a focus on the metabolic perspective","volume":"10","author":"Eisenreich","year":"2021","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1038\/cr.2015.68","article-title":"Metabolic reprogramming in macrophages and dendritic cells in innate immunity","volume":"25","author":"Kelly","year":"2015","journal-title":"Cell Res."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.micinf.2016.11.003","article-title":"Hypoxia and HIF-1 activation in bacterial infections","volume":"19","author":"Devraj","year":"2017","journal-title":"Microbes Infect."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"3531","DOI":"10.1128\/MCB.05124-11","article-title":"Hypoxia triggers AMPK activation through reactive oxygen species-mediated activation of calcium release-activated calcium channels","volume":"31","author":"Mungai","year":"2011","journal-title":"Mol. Cell. Biol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"2260","DOI":"10.1111\/febs.13270","article-title":"The impact of hypoxia on bacterial infection","volume":"282","author":"Schaffer","year":"2015","journal-title":"FEBS J."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"640901","DOI":"10.3389\/fvets.2021.640901","article-title":"Evidence of mitochondrial dysfunction in bacterial chondronecrosis with osteomyelitis\u2013affected broilers","volume":"8","author":"Ferver","year":"2021","journal-title":"Front. Vet. Sci."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"467","DOI":"10.3389\/fcell.2020.00467","article-title":"Mitophagy, mitochondrial homeostasis, and cell fate","volume":"8","author":"Ma","year":"2020","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"101","DOI":"10.3389\/fcimb.2013.00101","article-title":"Apoptosis-associated uncoupling of bone formation and resorption in osteomyelitis","volume":"3","author":"Marriott","year":"2013","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1007\/BF01908197","article-title":"Atrial bioenergetic variations in moderate hypoxia: Danger or protective defense?","volume":"84","author":"Caparrotta","year":"1989","journal-title":"Basic Res. Cardiol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1016\/j.yjmcc.2014.06.013","article-title":"Hypoxia signaling controls postnatal changes in cardiac mitochondrial morphology and function","volume":"74","author":"Ng","year":"2014","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"115568","DOI":"10.1016\/j.bone.2020.115568","article-title":"Intracellular Staphylococcus aureus in bone and joint infections: A mechanism of disease recurrence, inflammation, and bone and cartilage destruction","volume":"141","author":"Alder","year":"2020","journal-title":"Bone"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"918","DOI":"10.1302\/0301-620X.85B6.13509","article-title":"Intracellular Staphylococcus aureus. A mechanism for the indolence of osteomyelitis","volume":"85","author":"Ellington","year":"2003","journal-title":"J. Bone Jt. Surg. Br. Vol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"258","DOI":"10.22203\/eCM.v028a18","article-title":"Intracellular proliferation of S. aureus in osteoblasts and effects of rifampicin and gentamicin on S. aureus intracellular proliferation and survival","volume":"28","author":"Mohamed","year":"2014","journal-title":"Eur. Cells Mater."},{"key":"ref_124","doi-asserted-by":"crossref","unstructured":"Mohamed, W., Domann, E., Chakraborty, T., Mannala, G., Lips, K.S., Heiss, C., Schnettler, R., and Alt, V. (2016). TLR9 mediates S. aureus killing inside osteoblasts via induction of oxidative stress. BMC Microbiol., 16.","DOI":"10.1186\/s12866-016-0855-8"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"1343","DOI":"10.2106\/JBJS.D.02649","article-title":"Internalization of bacteria by osteoblasts in a patient with recurrent, long-term osteomyelitis: A case report","volume":"87","author":"Bosse","year":"2005","journal-title":"JBJS Case Connect."},{"key":"ref_126","doi-asserted-by":"crossref","unstructured":"Brunton, J., Steele, S., Ziehr, B., Moorman, N., and Kawula, T. (2013). Feeding uninvited guests: mTOR and AMPK set the table for intracellular pathogens. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003552"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"C775","DOI":"10.1152\/ajpcell.00279.2015","article-title":"Regulation of cell proliferation by hypoxia-inducible factors","volume":"309","author":"Hubbi","year":"2015","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1126\/science.aab4138","article-title":"Metabolism. AMP-activated protein kinase mediates mitochondrial fission in response to energy stress","volume":"351","author":"Toyama","year":"2016","journal-title":"Science"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"5197","DOI":"10.1093\/emboj\/20.18.5197","article-title":"Independent function of two destruction domains in hypoxia-inducible factor-\u03b1 chains activated by prolyl hydroxylation","volume":"20","author":"Masson","year":"2001","journal-title":"EMBO J."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/emm.2004.1","article-title":"Hypoxia-inducible factor (HIF-1)\u03b1: Its protein stability and biological functions","volume":"36","author":"Lee","year":"2004","journal-title":"Exp. Mol. Med."},{"key":"ref_131","doi-asserted-by":"crossref","unstructured":"Werth, N., Beerlage, C., Rosenberger, C., Yazdi, A.S., Edelmann, M., Amr, A., Bernhardt, W., von Eiff, C., Becker, K., and Sch\u00e4fer, A. (2010). Activation of hypoxia inducible factor 1 is a general phenomenon in infections with human pathogens. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0011576"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1002\/eji.201242765","article-title":"Genetic deletion of the HIF-1\u03b1 isoform I.1 in T cells enhances antibacterial immunity and improves survival in a murine peritonitis model","volume":"43","author":"Georgiev","year":"2013","journal-title":"Eur. J. Immunol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.joen.2018.10.007","article-title":"Endodontic infection-induced inflammation resembling osteomyelitis of the jaws in toll-like receptor 2\/Interleukin 10 double-knockout mice","volume":"45","author":"Sasaki","year":"2019","journal-title":"J. Endod."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"101109","DOI":"10.1016\/j.redox.2019.101109","article-title":"HIF-1\u03b1 protects against oxidative stress by directly targeting mitochondria","volume":"25","author":"Li","year":"2019","journal-title":"Redox Biol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"2977","DOI":"10.1016\/j.bbamcr.2016.09.012","article-title":"Activation of apoptosis signalling pathways by reactive oxygen species","volume":"1863","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"2012","DOI":"10.1161\/CIRCULATIONAHA.109.906610","article-title":"Inhibiting mitochondrial fission protects the heart against ischemia\/reperfusion injury","volume":"121","author":"Ong","year":"2010","journal-title":"Circulation"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"43","DOI":"10.3389\/fcimb.2012.00043","article-title":"Intracellular Staphylococcus aureus: Live-in and let die","volume":"2","author":"Fraunholz","year":"2012","journal-title":"Front. Cell. Infect. Microbiol."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/23\/9\/4571\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T22:57:50Z","timestamp":1760137070000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/23\/9\/4571"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,4,20]]},"references-count":137,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2022,5]]}},"alternative-id":["ijms23094571"],"URL":"https:\/\/doi.org\/10.3390\/ijms23094571","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,4,20]]}}}