About: Jean-Paul Renaud

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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) ikertzailea (eu) researcher (en) 연구원 (ko) 研究者 (ja) araştırmacı (tr) wetenschapper (nl) дослідник (uk) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy)
rdfs:label	Jean-Paul Renaud (en) Jean-Paul Renaud (es) Jean-Paul Renaud (nl) Jean-Paul Renaud (ast)
skos:prefLabel	Jean-Paul Renaud (en) Jean-Paul Renaud (es) Jean-Paul Renaud (nl) Jean-Paul Renaud (ast)
name	Jean-Paul Renaud (en) Jean-Paul Renaud (es) Jean-Paul Renaud (nl) Jean-Paul Renaud (ast)
given name	wds:Q56480056-145B2299-7A18-46B2-8272-CBA9B7F70334
given name	Jean-Paul
instance of	wds:Q56480056-2C1A65C5-3A7A-4E18-9005-031A9F4CF945
instance of	Homo sapiens
doctoral advisor	wds:Q56480056-068A2CC4-4304-4E4D-B9F5-D233B2A11B57
doctoral advisor	Daniel Mansuy
occupation	wds:Q56480056-1D2929FC-51DF-4B0E-A78D-74CFA20AF0AA
sex or gender	wds:Q56480056-AD585FC1-648C-4EC1-AED7-CA716176CC92
ISNI	wds:Q56480056-C7C207E4-4512-42CE-A511-DB710A9214D0
VIAF ID	wds:Q56480056-1D0C18CD-B150-46C4-A97E-436F4B98984C
GND ID	wds:Q56480056-c084e4b5-feb7-45b8-a823-3d0d6c49ac42
IdRef ID	wds:Q56480056-29884CC1-147B-4E81-8C73-D69998D38C0E
VIAF ID	http://viaf.org/viaf/49284653
GND ID	https://d-nb.info/gnd/1207794678
IdRef ID	http://www.idref.fr/031538614/id
occupation	researcher
sex or gender	male
ISNI	0000000000281405
VIAF ID	49284653
GND ID	1207794678
IdRef ID	031538614
ORCID iD	wds:Q56480056-D4EAFF7A-E7DC-4AAA-9323-DA3F461BA1F6
ORCID iD	https://orcid.org/0000-0001-9180-5426
ORCID iD	0000-0001-9180-5426
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q56480056
is author of	One Question, Multiple Answers: Biochemical and Biophysical Screening Methods Retrieve Deviating Fragment Hit Lists Retinoic acid receptor: a simulation analysis of retinoic acid binding and the resulting conformational changes Purification of the human RARgamma ligand-binding domain and crystallization of its complex with all-trans retinoic acid. A canonical structure for the ligand-binding domain of nuclear receptors Structural studies on nuclear receptors. A canonical structure for the ligand-binding domain of nuclear receptors Cisplatin- and UV-damaged DNA lure the basal transcription factor TFIID/TBP. X-ray structure of the orphan nuclear receptor RORbeta ligand-binding domain in the active conformation. International Union of Pharmacology. LXVI. Orphan nuclear receptors In silico fragment-based drug discovery: setup and validation of a fragment-to-lead computational protocol using S4MPLE. 3,5-T2 is an alternative ligand for the thyroid hormone receptor β1. Recombinant yeast in drug metabolism. Structure-function analysis reveals the molecular determinants of the impaired biological function of DAX-1 mutants in AHC patients Amphioxus postembryonic development reveals the homology of chordate metamorphosis. Structural basis for the inhibition of histone deacetylase 8 (HDAC8), a key epigenetic player in the blood fluke Schistosoma mansoni Structure-function analysis of the Rev-erbA and RVR ligand-binding domains reveals a large hydrophobic surface that mediates corepressor binding and a ligand cavity occupied by side chains Thermodynamic studies of substrate binding and spin transitions in human cytochrome P-450 3A4 expressed in yeast microsomes. Conformational heterogeneity of cytochrome P450 3A4 revealed by high pressure spectroscopy. All-trans retinoic acid is a ligand for the orphan nuclear receptor ROR beta Stereochemistry of carbon monoxide binding to normal human adult and Cowtown haemoglobins Biophysics in drug discovery: impact, challenges and opportunities. Particular ability of liver P450s3A to catalyze the oxidation of N omega-hydroxyarginine to citrulline and nitrogen oxides and occurrence in no synthases of a sequence very similar to the heme-binding sequence in P450s Binding of ligands and activation of transcription by nuclear receptors. High affinity of ergopeptides for cytochromes P450 3A. Importance of their peptide moiety for P450 recognition and hydroxylation of bromocriptine Cryo-EM in drug discovery: achievements, limitations and prospects Effect of the distal residues on the vibrational modes of the Fe-CO bond in hemoglobin studied by protein engineering Characterization of novel checkpoint kinase 1 inhibitors by in vitro assays and in human cancer cells treated with topoisomerase inhibitors.
is author of	wds:Q27680126-53E99BF1-C4EA-4922-ACCE-10997871195B wds:Q44406700-0B754413-4052-45C0-8B71-385F49EDA8ED wds:Q61818643-D67FEDE5-0436-4209-BEE6-962D7AC955A5 wds:Q72119079-D70CE372-B1C7-4F7D-9391-D6FA8A6D80A9 wds:Q35741775-264D1FD1-C46D-44DB-A972-50BC66DC69CD wds:Q57178721-B43EE087-A50B-4899-B0BA-108A30585F41 wds:Q33954013-14142287-DCC4-447E-8B58-0E07A291312A wds:Q34243256-75017836-4DA2-4DFB-8564-B344C3F87D90 wds:Q46565885-EF0D659F-A565-4DD2-A9FD-74356C4DFB5B wds:Q28276191-C33558FB-289B-45D1-A2C2-4D2CBF504983 wds:Q36102317-578C8ABD-8839-45DF-BF97-AFE56D076CED wds:Q42984304-83E45B85-C624-47CB-B8DC-FB76A78746CF wds:Q39143955-A1AA20FB-D063-4C6D-BBFB-159AEEE6CD8D wds:Q73788326-8C5A5AEA-1987-4802-8E25-C46D205D5500 wds:Q72077563-A656A808-4AB6-4676-9284-D92E579B5B56 wds:Q70907214-F9EBE975-60B9-4214-8A7B-244366C74F6C wds:Q38339920-4BCA1372-3C51-47EE-BE91-FEEF5C68C382 wds:Q68534423-755CD120-1EEF-47E6-AF01-C949F5F9EDDA wds:Q24535893-58ED0402-49B8-4790-90B6-6377BE80F840 wds:Q34640307-CC16512B-69AA-4BF9-99FD-B274D0B8A284 wds:Q34113739-1702BBB1-FAA2-4D1C-8C7F-0C5E0CA4DC3F wds:Q27641966-75268B92-0882-41B9-9130-F941C20ADA90 wds:Q38349347-466416E0-E7A9-4469-9AF4-82F92EEC53D5 wds:Q39403869-4C70ABC5-EAAE-4F7B-B3CE-ADB5FA8190C1

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