About: Steven Gamblin

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

biologist

Attributes	Values
rdf:type	Item
description	forskare (sv) biologo (it) ikertzailea (eu) 연구원 (ko) biologist (en) 研究者 (ja) araştırmacı (tr) wetenschapper (nl) дослідник (uk) изилдөөчү (ky) 研究者 (zh)
rdfs:label	Steven Gamblin (en) Steven J. Gamblin (es) Steven J. Gamblin (it) Steven J. Gamblin (nl) Steven J. Gamblin (sl) Steven J. Gamblin (ast)
skos:prefLabel	Steven Gamblin (en) Steven J. Gamblin (es) Steven J. Gamblin (it) Steven J. Gamblin (nl) Steven J. Gamblin (sl) Steven J. Gamblin (ast)
name	Steven Gamblin (en) Steven J. Gamblin (es) Steven J. Gamblin (it) Steven J. Gamblin (nl) Steven J. Gamblin (sl) Steven J. Gamblin (ast)
Scopus author ID	wds:Q21166090-bf96fdcb-42fe-8e44-b8f8-08f3de964867
Scopus author ID	7003313646
given name	wds:Q21166090-68F5FF6D-2904-44FF-AC69-26154ABDF519
given name	Steven
instance of	wds:Q21166090-260A1315-8DE0-4890-B625-43F20D6046F9
instance of	Homo sapiens
award received	wds:Q21166090-40b9037e-479f-8a8d-a704-e5f0bcbc2911 wds:Q21166090-63b94812-45e9-598f-7b31-46a2c1e64f23 wds:Q21166090-89B22356-8E9A-4857-AD9C-8B7C37E11A4D wds:Q21166090-c5cea8ed-4876-fd9f-fa89-8451d9a4aaec
award received	Fellow of the Royal Society Fellow of the Academy of Medical Sciences Feldberg Foundation Commander of the Order of the British Empire
Fellow of the Royal Society ID	wds:Q21166090-cbe74c0d-4c28-cb76-850e-9140d7cd9683
Fellow of the Royal Society ID	11477
skos:altLabel	Steven J. Gamblin (en)
occupation	wds:Q21166090-1B57127F-7ABC-4C8A-8FD2-88436D4658B2
employer	wds:Q21166090-1557aa46-4bea-75db-7e92-f5e508de7759 wds:Q21166090-B004ADB5-B161-443D-B163-83ACAFA90DAB
sex or gender	wds:Q21166090-D1B940DA-37A5-45B3-87B4-6BF0E7125EFE
member of	wds:Q21166090-ADF565D9-102B-4C51-8F5F-6B238E7C15CB
Who's Who UK ID	wds:Q21166090-e5ad1643-40b4-1dd9-72d2-1dccba2c8c6f
date of birth	wds:Q21166090-A28758E4-5930-40F4-87D4-483EE25162DD
family name	wds:Q21166090-294B6046-F6CC-4F7D-9A15-479F3950156B
occupation	researcher
employer	Francis Crick Institute
sex or gender	male
member of	Royal Society
Who's Who UK ID	U257472
date of birth	1962-01-07 00:00:00Z (xsd:dateTime)
family name	Gamblin
Springer Nature person ID	wds:Q21166090-A85B69F5-FEE0-41D1-B524-DC79ADFAD02C
ORCID iD	wds:Q21166090-21C707D2-9556-46D2-B9DA-5FA6C87375C7
Dimensions author ID	wds:Q21166090-D988418B-0F53-407B-853A-61C8FC8C7D9E
ORCID iD	https://orcid.org/0000-0001-5331-639X
Springer Nature person ID	014166377647.07
ORCID iD	0000-0001-5331-639X
Dimensions author ID	014166377647.07
is owl:sameAs of	Steven Gamblin
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q21166090
is author of	MgF(3)(-) as a transition state analog of phosphoryl transfer Jarid2 Methylation via the PRC2 Complex Regulates H3K27me3 Deposition during Cell Differentiation. AMP-activated protein kinase: nature's energy sensor Structural basis for AMP binding to mammalian AMP-activated protein kinase Activity and specificity of human aldolases Structure and mechanism of DNA topoisomerase II Haemagglutinin mutations responsible for the binding of H5N1 influenza A viruses to human-type receptors Structure and catalytic mechanism of the human histone methyltransferase SET7/9 Regulation of p53 activity through lysine methylation Crystal structure and functional analysis of the histone methyltransferase SET7/9 SET domains and histone methylation. The structure of simian virus 40 refined at 3.1 A resolution Recent evolution of equine influenza and the origin of canine influenza Crystal structure of the LasA virulence factor from Pseudomonas aeruginosa: substrate specificity and mechanism of M23 metallopeptidases Receptor binding by an H7N9 influenza virus from humans Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways Structure of mammalian AMPK and its regulation by ADP AMP-activated protein kinase: also regulated by ADP? Receptor binding by a ferret-transmissible H5 avian influenza virus Structure of the TPR domain of p67phox in complex with Rac.GTP GTPase-activating proteins and their complexes. Structural basis of oncogenic histone H3K27M inhibition of human polycomb repressive complex 2. Reading, writing and editing methylated lysines on histone tails: new insights from recent structural studies Antibiotic recognition by binuclear metallo-beta-lactamases revealed by X-ray crystallography The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Role of the polycomb protein EED in the propagation of repressive histone marks ADP Regulates SNF1, the Saccharomyces cerevisiae Homolog of AMP-Activated Protein Kinase Specificity determinants of recruitment peptides bound to phospho-CDK2/cyclin A

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