About: Jerry Vockley

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

Medical Genetics researcher

Attributes	Values
rdf:type	Item
description	forskare (sv) ikertzailea (eu) 연구원 (ko) গবেষক (bn) 研究者 (ja) ഗവേഷകൻ (ml) araştırmacı (tr) wetenschapper (nl) дослідник (uk) वैज्ञानिक (hi) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy) hulumtues (sq) Medical Genetics researcher (en)
rdfs:label	Jerry Vockley (en) Jerry Vockley (es) Jerry Vockley (it) Jerry Vockley (nl) Jerry Vockley (sl) Jerry Vockley (ast)
skos:prefLabel	Jerry Vockley (en) Jerry Vockley (es) Jerry Vockley (it) Jerry Vockley (nl) Jerry Vockley (sl) Jerry Vockley (ast)
name	Jerry Vockley (en) Jerry Vockley (es) Jerry Vockley (it) Jerry Vockley (nl) Jerry Vockley (sl) Jerry Vockley (ast)
Scopus author ID	wds:Q42112236-C726B288-829F-45B6-907A-20D911BC2D7F
Scopus author ID	7004917963
given name	wds:Q42112236-1C4E68BF-A844-4F84-B768-A4AF9C9269D1
given name	Jerry
instance of	wds:Q42112236-16A8B6B0-7EB0-4ECB-9A3E-66B67B8B9FD1
instance of	Homo sapiens
award received	wds:Q42112236-457f1184-4ae3-71ef-3b3c-d4f2385a343a
award received	Fellow of the American Association for the Advancement of Science
Loop ID	wds:Q42112236-20B69BC8-D10E-453A-9BEF-23AA40A70136
Loop ID	758363
skos:altLabel	Gerard Vockley (en)
occupation	wds:Q42112236-D900F6DF-7BFD-467A-8C71-CDBC9CBB4877
employer	wds:Q42112236-18515EDC-E03A-412C-B8EB-8B5583CEBAE9 wds:Q42112236-4318B509-A07C-47E2-B664-430A758B9799 wds:Q42112236-AC48BC21-E1B6-4E26-87D6-96AAB468BB85 wds:Q42112236-CD24104E-273E-4364-9CDE-7BD97ED0D49C wds:Q42112236-E96D0E4F-38C0-40FF-8665-ED38004FD459
sex or gender	wds:Q42112236-D2304454-0780-4877-9ED5-01104D5A9604
occupation	researcher
employer	University of Pittsburgh School of Medicine Yale School of Medicine Mayo Clinic University of Pittsburgh University of Pittsburgh Graduate School of Public Health
sex or gender	male
ORCID iD	wds:Q42112236-FB6988ED-2FA8-4984-BC15-05BFE3B10579
Dimensions author ID	wds:Q42112236-62F1FE15-0A29-4691-9091-0EB584EB96D9
ORCID iD	https://orcid.org/0000-0002-8180-6457
ORCID iD	0000-0002-8180-6457
Dimensions author ID	01114453306.24
ResearcherID	wds:Q42112236-A2F45C68-54CC-4ABE-B2CD-C2A9331B145F
Publons author ID	wds:Q42112236-eb309b88-14bb-4851-995e-695b9fe25e7e
ResearcherID	B-5210-2016
Publons author ID	2312089
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q42112236
is author of	Effects of diet and physical activity interventions on weight loss and cardiometabolic risk factors in severely obese adults: a randomized trial Medium-chain acyl-CoA dehydrogenase deficiency in gene-targeted mice Nutritional interventions in primary mitochondrial disorders: Developing an evidence base. Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases Short-chain acyl-CoA dehydrogenase gene mutation (c.319C>T) presents with clinical heterogeneity and is candidate founder mutation in individuals of Ashkenazi Jewish origin The ACADS gene variation spectrum in 114 patients with short-chain acyl-CoA dehydrogenase (SCAD) deficiency is dominated by missense variations leading to protein misfolding at the cellular level Purification and characterization of two polymorphic variants of short chain acyl-CoA dehydrogenase reveal reduction of catalytic activity and stability of the Gly185Ser enzyme Rare disorders of metabolism with elevated butyryl- and isobutyryl-carnitine detected by tandem mass spectrometry newborn screening Recurrent vomiting and ethylmalonic aciduria associated with rare mutations of the short-chain acyl-CoA dehydrogenase gene Misfolding, degradation, and aggregation of variant proteins. The molecular pathogenesis of short chain acyl-CoA dehydrogenase (SCAD) deficiency Synergistic heterozygosity in mice with inherited enzyme deficiencies of mitochondrial fatty acid beta-oxidation Acute fatty liver of pregnancy associated with short-chain acyl-coenzyme A dehydrogenase deficiency A new genetic disorder in mitochondrial fatty acid beta-oxidation: ACAD9 deficiency Human acyl-CoA dehydrogenase-9 plays a novel role in the mitochondrial beta-oxidation of unsaturated fatty acids Defects of mitochondrial beta-oxidation: a growing group of disorders. Human long chain, very long chain and medium chain acyl-CoA dehydrogenases are specific for the S-enantiomer of 2- methylpentadecanoyl-CoA Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans Isolation and expression of a cDNA encoding the precursor for a novel member (ACADSB) of the acyl-CoA dehydrogenase gene family Sirtuin 3 (SIRT3) protein regulates long-chain acyl-CoA dehydrogenase by deacetylating conserved lysines near the active site Molecular and clinical characterization of a recurrent cryptic unbalanced t(4q;18q) resulting in an 18q deletion and 4q duplication. Convergent evolution of a 2-methylbutyryl-CoA dehydrogenase from isovaleryl-CoA dehydrogenase in Solanum tuberosum Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase Metabolism as a complex genetic trait, a systems biology approach: implications for inborn errors of metabolism and clinical diseases Increased levels of plasma acylcarnitines in obesity and type 2 diabetes and identification of a marker of glucolipotoxicity. Women have higher protein content of beta-oxidation enzymes in skeletal muscle than men. High-level expression of an altered cDNA encoding human isovaleryl-CoA dehydrogenase in Escherichia coli Complex changes in the liver mitochondrial proteome of short chain acyl-CoA dehydrogenase deficient mice Metabolomic profiling of fatty acid and amino acid metabolism in youth with obesity and type 2 diabetes: evidence for enhanced mitochondrial oxidation. Barriers to the successful treatment of liver disease by hepatocyte transplantation Thermodynamic regulation of human short-chain acyl-CoA dehydrogenase by substrate and product binding Targeted disruption of mouse long-chain acyl-CoA dehydrogenase gene reveals crucial roles for fatty acid oxidation

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