{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T08:46:26Z","timestamp":1791276386199,"version":"4.1.0"},"reference-count":83,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2016,1,1]],"date-time":"2016-01-01T00:00:00Z","timestamp":1451606400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":["clinicalkey.jp","clinicalkey.com","cell.com","clinicalkey.es","clinicalkey.com.au","clinicalkey.fr","bmn.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Trends in Endocrinology &amp; Metabolism"],"published-print":{"date-parts":[[2016,1]]},"DOI":"10.1016\/j.tem.2015.11.003","type":"journal-article","created":{"date-parts":[[2015,12,2]],"date-time":"2015-12-02T05:19:40Z","timestamp":1449033580000},"page":"24-34","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":116,"title":["Targeting Insulin-Degrading Enzyme to Treat Type 2 Diabetes Mellitus"],"prefix":"10.1016","volume":"27","author":[{"given":"Wei-Jen","family":"Tang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.tem.2015.11.003_bib0005","first-page":"608","article-title":"Insulin degradation: progress and potential","volume":"19","author":"Duckworth","year":"1998","journal-title":"Endocr. Rev."},{"key":"10.1016\/j.tem.2015.11.003_bib0010","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/S0968-0004(01)01876-X","article-title":"Insulin-degrading enzyme: embarking on amyloid destruction","volume":"26","author":"Kurochkin","year":"2001","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.tem.2015.11.003_bib0015","doi-asserted-by":"crossref","first-page":"2574","DOI":"10.1007\/s00018-008-8112-4","article-title":"Amyloid \u03b2-degrading cryptidases: insulin degrading enzyme, presequence peptidase, and neprilysin","volume":"65","author":"Malito","year":"2008","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.tem.2015.11.003_bib0020","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1016\/j.neurobiolaging.2005.01.004","article-title":"Insulin, insulin-degrading enzyme and amyloid-\u03b2 peptide in Alzheimers disease: review and hypothesis","volume":"27","author":"Qiu","year":"2006","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.tem.2015.11.003_bib0025","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1038\/nature13297","article-title":"Anti-diabetic activity of insulin-degrading enzyme inhibitors mediated by multiple hormones","volume":"511","author":"Maianti","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.tem.2015.11.003_bib0030","first-page":"1","article-title":"The inactivation of insulin by tissue extracts; the distribution and properties of insulin inactivating extracts","volume":"20","author":"Mirsky","year":"1949","journal-title":"Arch. Biochem."},{"key":"10.1016\/j.tem.2015.11.003_bib0035","doi-asserted-by":"crossref","first-page":"14177","DOI":"10.1074\/jbc.M900068200","article-title":"Molecular basis of catalytic chamber-assisted unfolding and cleavage of human insulin by human insulin-degrading enzyme","volume":"284","author":"Manolopoulou","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tem.2015.11.003_bib0040","doi-asserted-by":"crossref","first-page":"2281","DOI":"10.1074\/jbc.M112.393108","article-title":"Insulin-degrading enzyme (IDE): a novel heat shock-like protein J","volume":"288","author":"Tundo","year":"2013","journal-title":"Biol. Chem."},{"key":"10.1016\/j.tem.2015.11.003_bib0045","doi-asserted-by":"crossref","first-page":"e95399","DOI":"10.1371\/journal.pone.0095399","article-title":"Regulation of insulin degrading enzyme activity by obesity-associated factors and pioglitazone in liver of diet-induced obese mice","volume":"9","author":"Wei","year":"2014","journal-title":"PLoS ONE"},{"key":"10.1016\/j.tem.2015.11.003_bib0050","doi-asserted-by":"crossref","first-page":"4670","DOI":"10.1074\/jbc.M110.173252","article-title":"Insulin-degrading enzyme modulates the natriuretic peptide-mediated signaling response","volume":"286","author":"Ralat","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tem.2015.11.003_bib0055","doi-asserted-by":"crossref","first-page":"e9719","DOI":"10.1371\/journal.pone.0009719","article-title":"A monomeric variant of insulin degrading enzyme (IDE) loses its regulatory properties","volume":"5","author":"Song","year":"2010","journal-title":"PLoS ONE"},{"key":"10.1016\/j.tem.2015.11.003_bib0060","doi-asserted-by":"crossref","first-page":"13827","DOI":"10.1073\/pnas.1304575110","article-title":"Conformational states and recognition of amyloidogenic peptides of human insulin-degrading enzyme","volume":"110","author":"McCord","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.tem.2015.11.003_bib0065","doi-asserted-by":"crossref","first-page":"13852","DOI":"10.1074\/jbc.M110.191668","article-title":"Mixed dimers of insulin-degrading enzyme reveal a cis activation mechanism","volume":"286","author":"Song","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tem.2015.11.003_bib0070","doi-asserted-by":"crossref","first-page":"54216","DOI":"10.1074\/jbc.M411177200","article-title":"ATP effects on insulin-degrading enzyme are mediated primarily through its triphosphate moiety","volume":"279","author":"Song","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tem.2015.11.003_bib0075","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1038\/nature05143","article-title":"Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism","volume":"443","author":"Shen","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.tem.2015.11.003_bib0080","doi-asserted-by":"crossref","first-page":"25453","DOI":"10.1074\/jbc.M701590200","article-title":"Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE","volume":"282","author":"Im","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tem.2015.11.003_bib0085","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1074\/jbc.M111.264614","article-title":"Anion activation site of insulin-degrading enzyme","volume":"287","author":"Noinaj","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tem.2015.11.003_bib0090","doi-asserted-by":"crossref","first-page":"3734","DOI":"10.1096\/fj.09-137455","article-title":"Structural changes in intermediate filament networks alter the activity of insulin-degrading enzyme","volume":"23","author":"Chou","year":"2009","journal-title":"FASEB J."},{"key":"10.1016\/j.tem.2015.11.003_bib0095","doi-asserted-by":"crossref","first-page":"e0132455","DOI":"10.1371\/journal.pone.0132455","article-title":"Proteasome activity is affected by fluctuations in insulin\u2013degrading enzyme distribution","volume":"10","author":"Sbardella","year":"2015","journal-title":"PLoS ONE"},{"key":"10.1016\/j.tem.2015.11.003_bib0100","doi-asserted-by":"crossref","first-page":"79","DOI":"10.3233\/JAD-2010-1206","article-title":"Insulin-degrading enzyme sorting in exosomes: a secretory pathway for a key brain amyloid-\u03b2 degrading protease","volume":"19","author":"Bulloj","year":"2010","journal-title":"J. Alzheimers Dis."},{"key":"10.1016\/j.tem.2015.11.003_bib0105","doi-asserted-by":"crossref","first-page":"37405","DOI":"10.1074\/jbc.M110.149468","article-title":"Statins promote the degradation of extracellular amyloid \u03b2-peptide by microglia via stimulation of exosome-associated insulin-degrading enzyme (ide) secretion","volume":"285","author":"Tamboli","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tem.2015.11.003_bib0110","doi-asserted-by":"crossref","first-page":"2330","DOI":"10.1242\/jcs.167270","article-title":"CALHM1 ion channel elicits amyloid-\u03b2 clearance by insulin-degrading enzyme in cell lines and in vivo in the mouse brain","volume":"128","author":"Vingtdeux","year":"2015","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.tem.2015.11.003_bib0115","doi-asserted-by":"crossref","first-page":"22711","DOI":"10.1074\/jbc.C110.217893","article-title":"Functional relevance of a novel SlyX motif in non-conventional secretion of insulin-degrading enzyme","volume":"286","author":"Glebov","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tem.2015.11.003_bib0120","doi-asserted-by":"crossref","first-page":"1802","DOI":"10.1172\/JCI29103","article-title":"Islet \u03b2 cell failure in type 2 diabetes","volume":"116","author":"Prentki","year":"2006","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.tem.2015.11.003_bib0125","doi-asserted-by":"crossref","first-page":"4162","DOI":"10.1073\/pnas.0230450100","article-title":"Insulin-degrading enzyme regulates the levels of insulin, amyloid beta-protein, and the beta-amyloid precursor protein intracellular domain in vivo","volume":"100","author":"Farris","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.tem.2015.11.003_bib0130","doi-asserted-by":"crossref","first-page":"1425","DOI":"10.1016\/S0002-9440(10)63229-4","article-title":"Partial loss-of-function mutations in insulin-degrading enzyme that induce diabetes also impair degradation of amyloid beta-protein","volume":"164","author":"Farris","year":"2004","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.tem.2015.11.003_bib0135","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/S1097-2765(05)00015-8","article-title":"Loss of insulin signaling in hepatocytes leads to severe insulin resistance and progressive hepatic dysfunction","volume":"6","author":"Michael","year":"2000","journal-title":"Mol. Cell"},{"key":"10.1016\/j.tem.2015.11.003_bib0140","doi-asserted-by":"crossref","first-page":"6221","DOI":"10.1073\/pnas.1031520100","article-title":"Amyloid-\u03b2 peptide levels in brain are inversely correlated with insulysin activity levels in vivo","volume":"100","author":"Miller","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.tem.2015.11.003_bib0145","doi-asserted-by":"crossref","first-page":"8250","DOI":"10.1038\/ncomms9250","article-title":"Catalytic site inhibition of insulin degrading enzyme by a small molecule induces glucose intolerance in mice","volume":"6","author":"Deprez\u2013poulain","year":"2015","journal-title":"Nat. Commun."},{"key":"10.1016\/j.tem.2015.11.003_bib0150","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1146\/annurev-nutr-071812-161201","article-title":"Incretins and amylin: neuroendocrine communication between the gut, pancreas, and brain in control of food intake and blood glucose","volume":"34","author":"Hayes","year":"2014","journal-title":"Annu. Rev. Nutr."},{"key":"10.1016\/j.tem.2015.11.003_bib0155","doi-asserted-by":"crossref","first-page":"E671","DOI":"10.1152\/ajpendo.00492.2002","article-title":"Glucagon and regulation of glucose metabolism","volume":"284","author":"Jiang","year":"2003","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"10.1016\/j.tem.2015.11.003_bib0160","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1210\/en.2011-1979","article-title":"Minireview: Glucagon in stress and energy homeostasis","volume":"153","author":"Jones","year":"2012","journal-title":"Endocrinology"},{"key":"10.1016\/j.tem.2015.11.003_bib0165","doi-asserted-by":"crossref","first-page":"e20818","DOI":"10.1371\/journal.pone.0020818","article-title":"Deletion of insulin-degrading enzyme elicits antipodal, age-dependent effects on glucose and insulin tolerance","volume":"6","author":"Abdul-Hay","year":"2011","journal-title":"PLoS ONE"},{"key":"10.1016\/j.tem.2015.11.003_bib0170","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1136\/jclinpath-2013-201515","article-title":"The role of amyloid \u03b2 in the pathogenesis of Alzheimer's disease","volume":"66","author":"Gilbert","year":"2013","journal-title":"J. Clin. Pathol."},{"key":"10.1016\/j.tem.2015.11.003_bib0175","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.tem.2015.11.003_bib0180","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1016\/S0896-6273(03)00787-6","article-title":"Enhanced proteolysis of \u03b2-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death","volume":"40","author":"Leissring","year":"2003","journal-title":"Neuron"},{"key":"10.1016\/j.tem.2015.11.003_bib0185","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1007\/s11684-013-0262-6","article-title":"Mechanisms of insulin resistance in obesity","volume":"7","author":"Ye","year":"2013","journal-title":"Front. Med."},{"key":"10.1016\/j.tem.2015.11.003_bib0190","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/S0896-6273(01)00475-5","article-title":"Clearing the brain's amyloid cobwebs","volume":"32","author":"Selkoe","year":"2001","journal-title":"Neuron"},{"key":"10.1016\/j.tem.2015.11.003_bib0195","doi-asserted-by":"crossref","first-page":"29645","DOI":"10.1074\/jbc.R800022200","article-title":"The A\u03b2Cs of A\u03b2-cleaving proteases","volume":"283","author":"Leissring","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tem.2015.11.003_bib0200","doi-asserted-by":"crossref","first-page":"996","DOI":"10.1016\/j.str.2014.05.003","article-title":"Molecular basis of substrate recognition and degradation by human presequence protease","volume":"22","author":"King","year":"2014","journal-title":"Structure"},{"key":"10.1016\/j.tem.2015.11.003_bib0205","first-page":"1174","article-title":"The Finland-United States investigation of non-insulin-dependent diabetes mellitus genetics (FUSION) study. I. An autosomal genome scan for genes that predispose to type 2 diabetes","volume":"67","author":"Ghosh","year":"2000","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.tem.2015.11.003_bib0210","doi-asserted-by":"crossref","first-page":"7825","DOI":"10.1074\/jbc.M609168200","article-title":"Decreased catalytic activity of the insulin-degrading enzyme in chromosome 10-linked Alzheimer disease families","volume":"282","author":"Kim","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tem.2015.11.003_bib0215","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1038\/nature05616","article-title":"A genome-wide association study identifies novel risk loci for type 2 diabetes","volume":"445","author":"Sladek","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.tem.2015.11.003_bib0220","doi-asserted-by":"crossref","first-page":"1336","DOI":"10.1126\/science.1142364","article-title":"Replication of genome-wide association signals in UK samples reveals risk loci for type 2 diabetes","volume":"316","author":"Zeggini","year":"2007","journal-title":"Science"},{"key":"10.1016\/j.tem.2015.11.003_bib0225","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1038\/ng.2915","article-title":"Loss-of-function mutations in SLC30A8 protect against type 2 diabetes","volume":"46","author":"Flannick","year":"2014","journal-title":"Nat. Genet."},{"key":"10.1016\/j.tem.2015.11.003_bib0230","doi-asserted-by":"crossref","first-page":"2302","DOI":"10.1126\/science.290.5500.2302","article-title":"Evidence for genetic linkage of Alzheimer's disease to chromosome 10q","volume":"290","author":"Bertram","year":"2000","journal-title":"Science"},{"key":"10.1016\/j.tem.2015.11.003_bib0235","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1038\/ng1934","article-title":"Systematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database","volume":"39","author":"Bertram","year":"2007","journal-title":"Nat. Genet."},{"key":"10.1016\/j.tem.2015.11.003_bib0240","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1002\/humu.10282","article-title":"Genetic variation in a haplotype block spanning IDE influences Alzheimer disease","volume":"22","author":"Prince","year":"2003","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.tem.2015.11.003_bib0245","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1016\/j.cell.2005.02.008","article-title":"Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective","volume":"120","author":"Tanzi","year":"2005","journal-title":"Cell"},{"key":"10.1016\/j.tem.2015.11.003_bib0250","doi-asserted-by":"crossref","first-page":"e8764","DOI":"10.1371\/journal.pone.0008764","article-title":"Concordant association of insulin degrading enzyme gene (IDE) variants with IDE mRNA, A\u03b2, and Alzheimer's disease","volume":"5","author":"Carrasquillo","year":"2010","journal-title":"PLoS ONE"},{"key":"10.1016\/j.tem.2015.11.003_bib0255","doi-asserted-by":"crossref","first-page":"1882","DOI":"10.1016\/j.biocel.2003.10.019","article-title":"Macrophage inflammatory protein-1","volume":"36","author":"Maurer","year":"2004","journal-title":"Int. J. Biochem. Cell B"},{"key":"10.1016\/j.tem.2015.11.003_bib0260","doi-asserted-by":"crossref","first-page":"3952","DOI":"10.1038\/emboj.2010.256","article-title":"Polymerization of MIP-1 chemokine (CCL3 and CCL4) and clearance of MIP-1 by insulin-degrading enzyme","volume":"29","author":"Ren","year":"2010","journal-title":"EMBO J."},{"key":"10.1016\/j.tem.2015.11.003_bib0265","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1038\/ni.1862","article-title":"Production of an antigenic peptide by insulin-degrading enzyme","volume":"11","author":"Parmentier","year":"2010","journal-title":"Nat. Immunol."},{"key":"10.1016\/j.tem.2015.11.003_bib0270","doi-asserted-by":"crossref","first-page":"8523","DOI":"10.1073\/pnas.1203195109","article-title":"Peptidomics approach to elucidate the proteolytic regulation of bioactive peptides","volume":"109","author":"Kim","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.tem.2015.11.003_bib0275","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1152\/physrev.00034.2013","article-title":"Calcitonin gene-related peptide: physiology and pathophysiology","volume":"94","author":"Russell","year":"2014","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.tem.2015.11.003_bib0280","doi-asserted-by":"crossref","first-page":"17039","DOI":"10.1074\/jbc.M706316200","article-title":"The catalytic domain of insulin-degrading enzyme forms a denaturant-resistant complex with amyloid \u03b2 peptide implications for Alzheimer disease","volume":"283","author":"Llovera","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tem.2015.11.003_bib0285","doi-asserted-by":"crossref","first-page":"2004","DOI":"10.2337\/db12-1045","article-title":"The type 2 diabetes-associated gene ide is required for insulin secretion and suppression of \u03b1-synuclein levels in \u03b2-cells","volume":"62","author":"Steneberg","year":"2013","journal-title":"Diabetes"},{"key":"10.1016\/j.tem.2015.11.003_bib0290","doi-asserted-by":"crossref","first-page":"12531","DOI":"10.1038\/srep12531","article-title":"Insulin-degrading enzyme prevents \u03b1-synuclein fibril formation in a nonproteolytical manner","volume":"5","author":"Sharma","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.tem.2015.11.003_bib0295","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/j.molmed.2015.04.005","article-title":"Type 2 diabetes as a protein misfolding disease","volume":"21","author":"Mukherjee","year":"2015","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.tem.2015.11.003_bib0300","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1146\/annurev.biochem.052308.114844","article-title":"Biological and chemical approaches to diseases of proteostasis deficiency","volume":"78","author":"Powers","year":"2009","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.tem.2015.11.003_bib0305","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1016\/j.jmb.2009.10.072","article-title":"Molecular basis for the recognition and cleavages of IGF-II, TGF-alpha, and amylin by human insulin-degrading enzyme","volume":"395","author":"Guo","year":"2010","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.tem.2015.11.003_bib0310","doi-asserted-by":"crossref","first-page":"12822","DOI":"10.1021\/bi801192h","article-title":"Molecular bases for the recognition of short peptide substrates and cysteine-directed modifications of human insulin-degrading enzyme","volume":"47","author":"Malito","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.tem.2015.11.003_bib0315","doi-asserted-by":"crossref","first-page":"e20864","DOI":"10.1371\/journal.pone.0020864","article-title":"Identification of the allosteric regulatory site of insulysin","volume":"6","author":"Noinaj","year":"2011","journal-title":"PLoS ONE"},{"key":"10.1016\/j.tem.2015.11.003_bib0320","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1126\/science.122.3169.559","article-title":"Effect of insulinase-inhibitor on hypoglycemic action of insulin","volume":"122","author":"Mirsky","year":"1955","journal-title":"Science"},{"key":"10.1016\/j.tem.2015.11.003_bib0325","doi-asserted-by":"crossref","first-page":"2315","DOI":"10.2337\/diabetes.52.9.2315","article-title":"An insulin-degrading enzyme inhibitor decreases amylin degradation, increases amylin-induced cytotoxicity, and increases amyloid formation in insulinoma cell cultures","volume":"52","author":"Bennett","year":"2003","journal-title":"Diabetes"},{"key":"10.1016\/j.tem.2015.11.003_bib0330","doi-asserted-by":"crossref","first-page":"e10504","DOI":"10.1371\/journal.pone.0010504","article-title":"Designed inhibitors of insulin-degrading enzyme regulate the catabolism and activity of insulin","volume":"5","author":"Leissring","year":"2010","journal-title":"PLoS ONE"},{"key":"10.1016\/j.tem.2015.11.003_bib0335","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.ejmech.2014.04.009","article-title":"Imidazole-derived 2-[N-carbamoylmethyl-alkylamino]acetic acids, substrate-dependent modulators of insulin-degrading enzyme in amyloid-\u03b2 hydrolysis","volume":"79","author":"Charton","year":"2014","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.tem.2015.11.003_bib0340","first-page":"547","article-title":"Structure-activity relationships of imidazole-derived 2-[N-carbamoylmethyl-alkylamino]acetic acids, dual binders of human insulin-degrading enzyme","volume":"90","author":"Charton","year":"2015","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.tem.2015.11.003_bib0345","doi-asserted-by":"crossref","first-page":"20044","DOI":"10.1074\/jbc.M115.638205","article-title":"Dual exosite-binding inhibitors of insulin-degrading enzyme challenge its role as the primary mediator of insulin clearance in vivo","volume":"290","author":"Durham","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tem.2015.11.003_bib0350","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/j.cmet.2014.07.016","article-title":"Insulin-degrading enzyme inhibition, a novel therapy for type 2 diabetes?","volume":"20","author":"Costes","year":"2014","journal-title":"Cell Metab."},{"key":"10.1016\/j.tem.2015.11.003_bib0355","doi-asserted-by":"crossref","first-page":"8850","DOI":"10.1073\/pnas.151261398","article-title":"Peripheral anti-A\u03b2 antibody alters CNS and plasma A\u03b2 clearance and decreases brain A\u03b2 burden in a mouse model of Alzheimer's disease","volume":"98","author":"DeMattos","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.tem.2015.11.003_bib0360","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1177\/1073858410381532","article-title":"Sink hypothesis and therapeutic strategies for attenuating A\u03b2 levels","volume":"17","author":"Zhang","year":"2011","journal-title":"Neuroscientist"},{"key":"10.1016\/j.tem.2015.11.003_bib0365","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.trci.2015.06.006","article-title":"Delayed-start analysis: Mild Alzheimer's disease patients in solanezumab trials, 3.5 years","volume":"1","author":"Liu-Seifert","year":"2015","journal-title":"Alzheimers Dement. Transl. Res. Clin. Interv."},{"key":"10.1016\/j.tem.2015.11.003_bib0370","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1016\/j.carpath.2013.03.006","article-title":"Insulin-degrading enzyme deficiency in bone marrow cells increases atherosclerosis in LDL receptor-deficient mice","volume":"22","author":"Caravaggio","year":"2013","journal-title":"Cardiovasc. Pathol."},{"key":"10.1016\/j.tem.2015.11.003_bib0375","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1210\/er.2007-0037","article-title":"Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis","volume":"29","author":"Haataja","year":"2008","journal-title":"Endocr. Rev."},{"key":"10.1016\/j.tem.2015.11.003_bib0380","doi-asserted-by":"crossref","first-page":"3629","DOI":"10.1210\/jc.2004-0405","article-title":"Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes","volume":"89","author":"Hull","year":"2004","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"10.1016\/j.tem.2015.11.003_bib0385","doi-asserted-by":"crossref","DOI":"10.1021\/acschembio.5b00334","article-title":"Selective targeting of extracellular insulin-degrading enzyme by quasi-irreversible thiol-modifying inhibitors","author":"Abdul-Hay","year":"2015","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.tem.2015.11.003_bib0390","series-title":"ML345, a Small-Molecule Inhibitor of the Insulin-Degrading Enzyme (IDE)","author":"Bannister","year":"2010"},{"key":"10.1016\/j.tem.2015.11.003_bib0395","doi-asserted-by":"crossref","first-page":"34005","DOI":"10.1074\/jbc.M109.030627","article-title":"Protective role of Cys-178 against the inactivation and oligomerization of human insulin-degrading enzyme by oxidation and nitrosylation","volume":"284","author":"Ralat","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tem.2015.11.003_bib0400","doi-asserted-by":"crossref","first-page":"15345","DOI":"10.1021\/bi050650l","article-title":"Susceptibility of amyloid \u03b2 peptide degrading enzymes to oxidative damage: a potential Alzheimer's disease spiral","volume":"44","author":"Shinall","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.tem.2015.11.003_bib0405","doi-asserted-by":"crossref","first-page":"e0133114","DOI":"10.1371\/journal.pone.0133114","article-title":"An extended polyanion activation surface in insulin degrading enzyme","volume":"10","author":"Song","year":"2015","journal-title":"PLoS ONE"},{"key":"10.1016\/j.tem.2015.11.003_bib0410","doi-asserted-by":"crossref","first-page":"e5274","DOI":"10.1371\/journal.pone.0005274","article-title":"Small-molecule activators of insulin-degrading enzyme discovered through high-throughput compound screening","volume":"4","author":"Cabrol","year":"2009","journal-title":"PLoS ONE"},{"key":"10.1016\/j.tem.2015.11.003_bib0415","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1186\/s13024-015-0054-3","article-title":"Statins induce insulin-degrading enzyme secretion from astrocytes via an autophagy-based unconventional secretory pathway","volume":"10","author":"Son","year":"2015","journal-title":"Mol. Neurodegener."}],"container-title":["Trends in Endocrinology &amp; Metabolism"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1043276015002180?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1043276015002180?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,9,17]],"date-time":"2018-09-17T07:52:51Z","timestamp":1537170771000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1043276015002180"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,1]]},"references-count":83,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2016,1]]}},"alternative-id":["S1043276015002180"],"URL":"https:\/\/doi.org\/10.1016\/j.tem.2015.11.003","relation":{},"ISSN":["1043-2760"],"issn-type":[{"value":"1043-2760","type":"print"}],"subject":[],"published":{"date-parts":[[2016,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Targeting Insulin-Degrading Enzyme to Treat Type 2 Diabetes Mellitus","name":"articletitle","label":"Article Title"},{"value":"Trends in Endocrinology & Metabolism","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.tem.2015.11.003","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2015 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}