About: Bishr Omary

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

medical researcher

Attributes	Values
rdf:type	Item
description	Forscher (de) forskare (sv) ikertzailea (eu) 연구원 (ko) ricercatore (it) 研究者 (ja) investigador (es) araştırmacı (tr) chercheur (fr) wetenschapper (nl) дослідник (uk) वैज्ञानिक (hi) изилдөөчү (ky) 研究者 (zh) medical researcher (en)
rdfs:label	Bishr Omary (en) M B Omary (es) M B Omary (nl) M B Omary (ast)
skos:prefLabel	Bishr Omary (en) M B Omary (es) M B Omary (nl) M B Omary (ast)
name	Bishr Omary (en) M B Omary (es) M B Omary (nl) M B Omary (ast)
Scopus author ID	wds:Q68064171-7A881A44-F84D-49C7-AC06-7A0F7731E085
Scopus author ID	7006210555
described by source	wds:Q68064171-619d69f0-4e7d-96b8-32f2-c0e7e7607900
instance of	wds:Q68064171-C3A1F4FE-3FD3-4ADB-8AAC-9E74794A7E30
described by source	Our New President-M. Bishr Omary, MD, PhD, AGAF
instance of	Homo sapiens
skos:altLabel	M. Bishr Omary, (en)
occupation	wds:Q68064171-8143C238-777E-4AFB-BEDD-C3E24A802B80
employer	wds:Q68064171-486cedb4-45b1-4600-ae6e-c94d7cdf69b5 wds:Q68064171-61694b9a-4140-627c-14e0-c767ee88a445
sex or gender	wds:Q68064171-12d12a77-1e1d-4bfc-8f85-49767d1e83cd
ISNI	wds:Q68064171-FACFA5F6-27CB-4F98-8A93-66B68B7F9E10
VIAF ID	wds:Q68064171-9F6291D0-8E94-49C5-8F5F-15B9260C4773
IdRef ID	wds:Q68064171-6d2f47e3-c22d-4d4d-aa1b-86e95e3715bd
National Library of Israel J9U ID	wds:Q68064171-ED0906A6-2275-4567-B775-42689197F046
VIAF ID	http://viaf.org/viaf/270612413
IdRef ID	http://www.idref.fr/083317937/id
occupation	researcher
employer	Rutgers University University of Michigan Medical School
sex or gender	male
ISNI	0000000050685088
VIAF ID	270612413
IdRef ID	083317937
National Library of Israel J9U ID	987007350529805171
ORCID iD	wds:Q68064171-2FE4D7F6-B88E-4E2F-B3DD-0ECC3A4A1313
ORCID iD	https://orcid.org/0000-0002-8624-2347
ORCID iD	0000-0002-8624-2347
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q68064171
is author of	Keratin 20 serine 13 phosphorylation is a stress and intestinal goblet cell marker Interferon-alpha induces nmi-IFP35 heterodimeric complex formation that is affected by the phosphorylation of IFP35 Keratin 8 modulates β-cell stress responses and normoglycaemia Keratin 8 absence down-regulates colonocyte HMGCS2 and modulates colonic ketogenesis and energy metabolism. Absence of keratin 8 or 18 promotes antimitochondrial autoantibody formation in aging male mice PKC epsilon-related kinase associates with and phosphorylates cytokeratin 8 and 18 Post-translational modifications of intermediate filament proteins: mechanisms and functions "IF-pathies": a broad spectrum of intermediate filament-associated diseases. Aggregation and loss of cytokeratin filament networks inhibit golgi organization in liver-derived epithelial cell lines. Absence of keratin 19 in mice causes skeletal myopathy with mitochondrial and sarcolemmal reorganization. New consensus nomenclature for mammalian keratins Association of glucose-regulated protein (grp78) with human keratin 8. Absence of keratin 8 confers a paradoxical microflora-dependent resistance to apoptosis in the colon. Cellular integrity plus: organelle-related and protein-targeting functions of intermediate filaments. Phosphorylation of human keratin 8 in vivo at conserved head domain serine 23 and at epidermal growth factor-stimulated tail domain serine 431 Phosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteins Keratin binding to 14-3-3 proteins modulates keratin filaments and hepatocyte mitotic progression Mutation of human keratin 18 in association with cryptogenic cirrhosis Keratin 8 phosphorylation by p38 kinase regulates cellular keratin filament reorganization: modulation by a keratin 1-like disease causing mutation Type II keratins are phosphorylated on a unique motif during stress and mitosis in tissues and cultured cells. Keratin 8 and 18 mutations are risk factors for developing liver disease of multiple etiologies. Keratins turn over by ubiquitination in a phosphorylation-modulated fashion Mutation of a major keratin phosphorylation site predisposes to hepatotoxic injury in transgenic mice A mutation of keratin 18 within the coil 1A consensus motif causes widespread keratin aggregation but cell type-restricted lethality in mice Keratin variants associate with progression of fibrosis during chronic hepatitis C infection Human cell surface glycoprotein related to cell proliferation is the receptor for transferrin Fibrinogen-γ proteolysis and solubility dynamics during apoptotic mouse liver injury: heparin prevents and treats liver damage. Keratin overexpression levels correlate with the extent of spontaneous pancreatic injury. Keratin 8/18 breakdown and reorganization during apoptosis. The intermediate filament protein keratin 8 is a novel cytoplasmic substrate for c-Jun N-terminal kinase. Autophagy activation by rapamycin eliminates mouse Mallory-Denk bodies and blocks their proteasome inhibitor-mediated formation. Human cell-surface glycoprotein with unusual properties. Hemin-activated macrophages home to the pancreas and protect from acute pancreatitis via heme oxygenase-1 induction Keratin 20 helps maintain intermediate filament organization in intestinal epithelia Keratin mutation in transgenic mice predisposes to Fas but not TNF-induced apoptosis and massive liver injury. T200 cell surface glycoprotein of the mouse. Polymorphism defined by the Ly-5 system of alloantigens. Characterization of the major physiologic phosphorylation site of human keratin 19 and its role in filament organization. Effect of sulindac on sporadic colonic polyps. Human homologue of murine T200 glycoprotein. Carbamoyl phosphate synthetase-1 is a rapid turnover biomarker in mouse and human acute liver injury Characterization of in vivo keratin 19 phosphorylation on tyrosine-391 Keratin hypersumoylation alters filament dynamics and is a marker for human liver disease and keratin mutation. Keratin variants predispose to acute liver failure and adverse outcome: race and ethnic associations.

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