About: Emanuel Margoliash

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

American biochemist (1920-2008)

Attributes	Values
rdf:type	Item
description	biocimiciste american (lfn) usona biokemiisto (eo) biochemicus (nl) American biochemist (1920-2008) (en)
rdfs:label	Emanuel Margoliash (de) Emanuel Margoliash (en) Emanuel Margoliash (es) Emanuel Margoliash (fr) Emanuel Margoliash (it) Emanuel Margoliash (nl) Emanuel Margoliash (sq) Emanuel Margoliash (ast) Емануель Марголіаш (uk)
skos:prefLabel	Emanuel Margoliash (de) Emanuel Margoliash (en) Emanuel Margoliash (es) Emanuel Margoliash (fr) Emanuel Margoliash (it) Emanuel Margoliash (nl) Emanuel Margoliash (sq) Emanuel Margoliash (ast) Емануель Марголіаш (uk)
name	Emanuel Margoliash (de) Emanuel Margoliash (en) Emanuel Margoliash (es) Emanuel Margoliash (fr) Emanuel Margoliash (it) Emanuel Margoliash (nl) Emanuel Margoliash (sq) Emanuel Margoliash (ast) Емануель Марголіаш (uk)
Freebase ID	wds:Q5369102-3C16CB1F-E0AB-4F90-AB3B-0D19153467E5
Freebase ID	/m/047stx2
National Academy of Sciences member ID	wds:Q5369102-a9da39c4-453b-2424-9c58-8b7f4285afa8
National Academy of Sciences member ID	52943
given name	wds:Q5369102-10ED0664-051C-4ED5-9C6E-E249CE78B270
given name	Immanuel
instance of	wds:Q5369102-2551A618-2964-4F8A-A991-9F0678684F95
instance of	Homo sapiens
award received	wds:Q5369102-2D761F20-05A1-4E96-8B0E-EDEFDE8C8D09
award received	Guggenheim Fellowship
Guggenheim fellows ID	wds:Q5369102-71CD8279-5FDE-4E01-B23D-7CB4FA9DB4C7
Guggenheim fellows ID	emanuel-margoliash
occupation	wds:Q5369102-c369861b-5ba1-492a-b303-3c541ae2575c
employer	wds:Q5369102-633AD79C-BCD3-46D6-881D-AF44E60FE622 wds:Q5369102-E34164A2-B697-4F59-90A6-5CC69A0626E2
place of birth	wds:Q5369102-069E87B6-3C40-4922-AA38-DEF3EF1A3E0E
sex or gender	wds:Q5369102-F0848F30-E89C-4F4A-B916-7CA42B4217EE
Prabook ID	wds:Q5369102-B7E0B1D5-89D8-4CAB-8AEC-1F1C20ED27E0
member of	wds:Q5369102-15855E7D-C2A2-49E3-81F0-8626FB1F57B7 wds:Q5369102-FC4D6AA9-6959-4FF8-8D6F-49F594B76BE5
date of birth	wds:Q5369102-294773CF-BE6C-42A5-B530-53532D96EC29
date of death	wds:Q5369102-7280092E-EB62-42B4-86BA-CE4969238EA8
educated at	wds:Q5369102-383DA31D-72A9-498C-8720-D5DD8D603DED
family name	wds:q5369102-a9915e18-407e-b9ac-6c64-a91c88798fa0
occupation	biochemist
employer	University of Illinois at Chicago University of Utah
place of birth	El Cairo
sex or gender	male
Prabook ID	646766
member of	National Academy of Sciences American Academy of Arts and Sciences
date of birth	1920-02-10 00:00:00Z (xsd:dateTime)
date of death	2008-04-10 00:00:00Z (xsd:dateTime)
educated at	American University of Beirut
family name	Margoliash
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q5369102 Emanuel Margoliash https://uk.wikipedia.org/wiki/%D0%95%D0%BC%D0%B0%D0%BD%D1%83%D0%B5%D0%BB%D1%8C_%D0%9C%D0%B0%D1%80%D0%B3%D0%BE%D0%BB%D1%96%D0%B0%D1%88
is author of	Remarkably high activities of testicular cytochrome c in destroying reactive oxygen species and in triggering apoptosis Multiple low spin forms of the cytochrome c ferrihemochrome. EPR spectra of various eukaryotic and prokaryotic cytochromes c A chemical modification of cytochrome-c lysines leading to changes in heme iron ligation Molecular expression of evolutinary phenomena in the primary and tertiary structures of cytochrome c. "Homology" in proteins and nucleic acids: a terminology muddle and a way out of it. Definition of cytochrome c binding domains by chemical modification. III. Kinetics of reaction of carboxydinitrophenyl cytochromes c with cytochrome c oxidase Amino acid sequence of a cytochrome c from the common Pacific lamprey, Entosphenus tridentatus Changing the invariant proline-30 of rat and Drosophila melanogaster cytochromes c to alanine or valine destabilizes the heme crevice more than the overall conformation Steady state kinetics and binding of eukaryotic cytochromes c with yeast cytochrome c peroxidase Effects of mutating Asn-52 to isoleucine on the haem-linked properties of cytochrome c. Kinetics and energetics of intramolecular electron transfer in yeast cytochrome c peroxidase 18 Mitochondrial cytochrome c: Preparation and activity of native and chemically modified cytochromes c A peptide binding protein having a role in antigen presentation is a member of the HSP70 heat shock family The Structure of Bovine Proinsulin Definition of cytochrome c binding domains by chemical modification. II. Identification and properties of singly substituted carboxydinitrophenyl cytochromes c at lysines 8, 13, 22, 27, 39, 60, 72, 87, and 99 The asymmetric distribution of charges on the surface of horse cytochrome c. Functional implications Definition of cytochrome c binding domains by chemical modification. I. Reaction with 4-chloro-3,5-dinitrobenzoate and chromatographic separation of singly substituted derivatives The reaction of primate cytochromes c with cytochrome c oxidase. Analysis of the polarographic assay Electrostatic interactions in cytochrome c. The role of interactions between residues 13 and 90 and residues 79 and 47 in stabilizing the heme crevice structure Construction of phylogenetic trees T-lymphocyte response to cytochrome c. I. Demonstration of a T-cell heteroclitic proliferative response and identification of a topographic antigenic determinant on pigeon cytochrome c whose immune recognition requires two complementing major histoc Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8 A resolution Characterization of the interaction of cytochrome c and mitochondrial ubiquinol-cytochrome c reductase. Peptides related to the antigenic determinant block T cell recognition of the native protein as processed by antigen-presenting cells Definitaion of cytochrome c binding domains by chemical modification. Reaction of carboxydinitrophenyl- and trinitrophenyl-cytochromes c with baker's yeast cytochrome c peroxidase Cytochrome c: Immunofluorescent Localization of the Testis-Specific Form Structural significance of an internal water molecule studied by site-directed mutagenesis of tyrosine-67 in rat cytochrome c. Proinsulin and the biosynthesis of insulin Electron paramagnetic and electron nuclear double resonance of the hydrogen peroxide compound of cytochrome c peroxidase

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