About: Opher Gileadi

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

researcher

Attributes	Values
rdf:type	Item
description	forskare (sv) researcher (en) 연구원 (ko) ricercatore (it) গবেষক (bn) 研究者 (ja) araştırmacı (tr) chercheur (fr) wetenschapper (nl) дослідник (uk) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy) researcher (en-ca) researcher (en-gb) researcher (en-us) investigador (ca) investigador (gl) investigador (ast) investigador (pt) investigador/a (es)
exact match	wds:Q38321459-501A3B8F-3B40-4348-9284-78D2975E527E
exact match	https://scigraph.springernature.com/person.01325717130.95
rdfs:label	Opher Gileadi (de) Opher Gileadi (en) Opher Gileadi (es) Opher Gileadi (fr) Opher Gileadi (nl) Opher Gileadi (sl) Opher Gileadi (ast) Opher Gileadi (bar)
skos:prefLabel	Opher Gileadi (de) Opher Gileadi (en) Opher Gileadi (es) Opher Gileadi (fr) Opher Gileadi (nl) Opher Gileadi (sl) Opher Gileadi (ast) Opher Gileadi (bar)
name	Opher Gileadi (de) Opher Gileadi (en) Opher Gileadi (es) Opher Gileadi (fr) Opher Gileadi (nl) Opher Gileadi (sl) Opher Gileadi (ast) Opher Gileadi (bar)
Scopus author ID	wds:Q38321459-42D78780-3EB3-4293-80C7-1CB2C77A9058 wds:Q38321459-EADC9ABB-1DE0-42B5-85B0-4CCBEBDCDF5B
Scopus author ID	6701748832
instance of	wds:Q38321459-F05BBECA-78EB-4C3D-81E6-BD5CEE77E24C
instance of	Homo sapiens
occupation	wds:Q38321459-2E21BDC6-4B5D-4145-9BED-D97C06B9CA9C
employer	wds:Q38321459-246C2663-012F-4382-994B-8AEA68292C97 wds:Q38321459-492A1772-11FA-424E-B76A-DD8D71EDBD51 wds:Q38321459-81847434-141A-44B5-9BF2-5E9FABD44FCA wds:Q38321459-C1B88E65-C4AD-4D78-AF4B-E0D1625065A7 wds:Q38321459-C974C0A1-1190-41C3-BA78-210379A78B31
date of birth	wds:Q38321459-E2C39E26-8832-4257-B8F1-3D4FAA4F8E24
educated at	wds:Q38321459-675FF3D3-08E1-4D1B-87E0-8459519181A4 wds:Q38321459-8B9933DD-27A1-40E8-AB80-D1BE6FFCD3DD
National Library of Israel J9U ID	wds:Q38321459-A0629038-687D-43B8-99B0-A8E634573A88
occupation	researcher
employer	Stanford University School of Medicine Karolinska Institutet University of Oxford Hebrew University of Jerusalem Weizmann Institute of Science
date of birth	2000-01-01 00:00:00Z (xsd:dateTime)
educated at	Hebrew University of Jerusalem
National Library of Israel J9U ID	987012651276305171
ORCID iD	wds:Q38321459-040EB6AC-BFB8-478F-9A23-0CE8203A8CAF
Dimensions author ID	wds:Q38321459-E2F32850-8FB0-4FF2-9FEA-72C436B41587
ORCID iD	https://orcid.org/0000-0001-6886-898X
ORCID iD	0000-0001-6886-898X
Dimensions author ID	01325717130.95
ResearcherID	wds:Q38321459-B012D755-149E-4CF6-B079-DDBD758B2B2A
Publons author ID	wds:Q38321459-a156c84f-0659-4ed6-a778-f277a17fcfce
ResearcherID	F-1105-2013
Publons author ID	2644559
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q38321459
is author of	An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae. Involvement of yeast carboxy-terminal domain kinase I (CTDK-I) in transcription elongation in vivo Transcription of the H19 gene in differentiating cytotrophoblasts from human placenta Codon optimization can improve expression of human genes in Escherichia coli: A multi-gene study. Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states Crystal structures of the catalytic domain of human soluble guanylate cyclase CTD kinase associated with yeast RNA polymerase II initiation factor b. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity Mutations in multidomain protein MEGF8 identify a Carpenter syndrome subtype associated with defective lateralization Crystal Structures of Malonyl-Coenzyme A Decarboxylase Provide Insights into Its Catalytic Mechanism and Disease-Causing Mutations Mutations in the RING domain of TFB3, a subunit of yeast transcription factor IIH, reveal a role in cell cycle progression Human SNM1A and XPF-ERCC1 collaborate to initiate DNA interstrand cross-link repair Structural Basis for Cul3 Protein Assembly with the BTB-Kelch Family of E3 Ubiquitin Ligases The scientific impact of the Structural Genomics Consortium: a protein family and ligand-centered approach to medically-relevant human proteins Isolated short CTG/CAG DNA slip-outs are repaired efficiently by hMutSbeta, but clustered slip-outs are poorly repaired Scanning electron microscopy of cells and tissues under fully hydrated conditions High-throughput production of human proteins for crystallization: the SGC experience. Structural and functional insights into the DNA replication factor Cdc45 reveal an evolutionary relationship to the DHH family of phosphoesterases

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