About: Pierre Béguin

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researcher

Attributes	Values
rdf:type	Item
description	ikertzailea (eu) researcher (en) 연구원 (ko) 研究者 (ja) araştırmacı (tr) дослідник (uk) эрдэмтэн (mn) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy) onderzoeker (nl)
rdfs:label	Pierre Béguin (en) Pierre Béguin (it) P Béguin (es) P Béguin (nl) P Béguin (sl) P Béguin (ast)
skos:prefLabel	Pierre Béguin (en) Pierre Béguin (it) P Béguin (es) P Béguin (nl) P Béguin (sl) P Béguin (ast)
name	Pierre Béguin (en) Pierre Béguin (it) P Béguin (es) P Béguin (nl) P Béguin (sl) P Béguin (ast)
Scopus author ID	wds:Q54065112-D93099FF-85A8-4191-AE03-6285FB5FD892
Scopus author ID	7004815865
given name	wds:Q54065112-09C69C71-AFE4-4C31-AFDE-FDF64A4A21AE
given name	Pierre
instance of	wds:Q54065112-9B0F3429-9211-4E9E-A2F9-CEE5481B85D6
instance of	Homo sapiens
doctoral student	wds:Q54065112-87DADFF5-4BF8-458E-9208-D33264330D05
doctoral student	Olivier Grépinet
occupation	wds:Q54065112-93E07DAE-1D7D-4C29-86F7-46759D5BC008
employer	wds:Q54065112-2DD14112-AEF3-4DAD-BA35-92CD209474BB wds:Q54065112-C451BEC8-7C52-4899-940C-F1CDEAEE6288
NUKAT ID	wds:Q54065112-92AAA6BD-DE68-46FD-8068-D3A4051753CD
sex or gender	wds:Q54065112-C0FEFB00-4D9D-45CA-85C6-55482642EF5C
ISNI	wds:Q54065112-3C2710C2-BE32-483D-82C6-295B667E0D20
VIAF ID	wds:Q54065112-884704F8-2296-49AB-9893-DFD5434D547A
IdRef ID	wds:Q54065112-45B3BA95-2663-4508-B775-B1B66A76AFC2
family name	wds:Q54065112-F5F3B390-9C77-4269-9EDB-585350FF2ACF
National Library of Israel J9U ID	wds:Q54065112-EC1CBFB9-E502-4D16-A242-9CACCB9D7A5B
VIAF ID	http://viaf.org/viaf/58171925
IdRef ID	http://www.idref.fr/19231095X/id
occupation	researcher
employer	Pasteur Institute Institut Pasteur de Lille
NUKAT ID	n2020147012
sex or gender	male
ISNI	0000000027314713
VIAF ID	58171925
IdRef ID	19231095X
family name	Béguin
National Library of Israel J9U ID	987007329412205171
ORCID iD	wds:Q54065112-36755A5F-01EC-48E5-A56F-5F60E8F5D62B
ORCID iD	https://orcid.org/0000-0002-5372-6281
ORCID iD	0000-0002-5372-6281
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q54065112
is author of	The crystal structure of a type I cohesin domain at 1.7 A resolution Site-directed mutagenesis of conserved residues of Clostridium thermocellum endoglucanase CelC Duplicated dockerin subdomains of Clostridium thermocellum endoglucanase CelD bind to a cohesin domain of the scaffolding protein CipA with distinct thermodynamic parameters and a negative cooperativity Nucleotide sequence of the cellulase gene celD encoding endoglucanase D of Clostridium thermocellum. Hybrid enzymes Purification and properties of the endoglucanase C of Clostridium thermocellum produced in Escherichia coli. Mapping of mRNA encoding endoglucanase A from Clostridium thermocellum Identification of the endoglucanase encoded by the celB gene of Clostridium thermocellum Atomic (0.94 A) resolution structure of an inverting glycosidase in complex with substrate Mapping by Site-Directed Mutagenesis of the Region Responsible for Cohesin−Dockerin Interaction on the Surface of the Seventh Cohesin Domain ofClostridium thermocellumCipA† Detection of cellulase activity in polyacrylamide gels using Congo red-stained agar replicas. Structural and Functional Analysis of the Metal-binding Sites ofClostridium thermocellumEndoglucanase CelD Functions of S-layers Nucleotide sequence of the cellulase gene celF of Clostridium thermocellum Cellulose degradation by Clostridium thermocellum: from manure to molecular biology Structural basis for a novel mechanism of DNA bridging and alignment in eukaryotic DSB DNA repair. High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D. Interaction of the duplicated segment carried by Clostridium thermocellum cellulases with cellulosome components Synergism between the cellulosome-integrating protein CipA and endoglucanase CelD of Clostridium thermocellum Cloning of a Clostridium thermocellum DNA fragment encoding polypeptides that bind the catalytic components of the cellulosome Involvement of separate domains of the cellulosomal protein S1 of Clostridium thermocellum in binding to cellulose and in anchoring of catalytic subunits to the cellulosome Crystallization and preliminary diffraction analysis of the catalytic domain of xylanase Z from Clostridium thermocellum. Cohesin-dockerin interactions within and between Clostridium josui and Clostridium thermocellum: binding selectivity between cognate dockerin and cohesin domains and species specificity. Synergistic template-free synthesis of dsDNA by Thermococcus nautili primase PolpTN2, DNA polymerase PolB, and pTN2 helicase Identification of conserved amino acid residues of the Salmonella sigmaS chaperone Crl involved in Crl-sigmaS interactions. A highly divergent archaeo-eukaryotic primase from the Thermococcus nautilus plasmid, pTN2. Crystallization and preliminary X-ray diffraction study of an endoglucanase from Clostridium thermocellum. Time- and temperature-dependent acetylation of the chemokine RANTES produced in recombinant Escherichia coli. Identification of N‐ and C‐terminal corticotropin peptides in the Mr 80 000 form of neurophysin The SF1 helicase encoded by the archaeal plasmid pTN2 of Thermococcus nautili. Cell-free synthesis of glial fibrillary acidic protein 1H, 13C, 15N NMR sequence-specific resonance assignment of a Clostridium thermocellum type II cohesin module Production of soluble, active acetyl serotonin methyl transferase in Leishmania tarentolae.
is author of	wds:Q67525312-A6355841-CD06-42CF-91FC-30EFB4DF7ED4 wds:Q42619903-C34E2F54-A157-4664-B5E1-C7C8D781C51E wds:Q54781211-4026E5C7-C81D-4728-B04B-700FAC1A4511

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