About: Udo Heinemann

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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) investigador (es) chercheur (fr) wetenschapper (nl) дослідник (uk) эрдэмтэн (mn) वैज्ञानिक (hi) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy) hulumtues (sq) ഗവേഷകന്‍ (ml) researcher (en-ca) researcher (en-gb) researcher (en-us) investigador (ca) investigador (gl) investigador (ast) investigador (pt)
rdfs:label	Udo Heinemann (en) Udo Heinemann (es) Udo Heinemann (fr) Udo Heinemann (it) Udo Heinemann (nl) Udo Heinemann (sl) Udo Heinemann (ast)
skos:prefLabel	Udo Heinemann (en) Udo Heinemann (es) Udo Heinemann (fr) Udo Heinemann (it) Udo Heinemann (nl) Udo Heinemann (sl) Udo Heinemann (ast)
name	Udo Heinemann (en) Udo Heinemann (es) Udo Heinemann (fr) Udo Heinemann (it) Udo Heinemann (nl) Udo Heinemann (sl) Udo Heinemann (ast)
Scopus author ID	wds:Q28037243-2786E7A3-3D97-44C0-8BD4-25BF6BFEFD62
Scopus author ID	7103045935
given name	wds:Q28037243-37AD4734-134E-401A-8BF0-83640EFA2FE4
given name	Udo
instance of	wds:Q28037243-9B75E7D6-EB4B-4340-99E2-A74157B3771B
instance of	Homo sapiens
occupation	wds:Q28037243-BABEBA6B-DCB4-4BCB-B27D-E7BB7BE38AB7
employer	wds:Q28037243-2116D9C8-000F-4025-B4F0-5E5769EEB0C8 wds:Q28037243-4AD7D733-6897-4FA1-B66F-ADA95B06888D wds:Q28037243-675BEDA4-D0EE-4D11-872D-7DA397808693 wds:Q28037243-F6F69090-2ECD-471F-8A65-D8B479ECAE6F
sex or gender	wds:Q28037243-9EFEE37E-E8CE-4136-BCC3-3303C6F6B394
VIAF ID	wds:Q28037243-4FFBCF38-7CA3-4E8F-8835-130623F88553
GND ID	wds:Q28037243-105dcafb-dab2-49e9-866a-bbc7d9b17128
date of birth	wds:Q28037243-B85FAD83-4BC8-4EE9-8473-BA90CE7122EF
family name	wds:Q28037243-D90F2A25-111C-47EE-8C14-B8D4E78782A6
WorldCat Identities ID (superseded)	wds:Q28037243-11F78DE9-BF9C-412F-B4C4-1BE094DD2AA9
VIAF ID	http://viaf.org/viaf/168053635
GND ID	https://d-nb.info/gnd/143582119
occupation	researcher
employer	University of California, Los Angeles Free University Berlin University of Stuttgart Max Delbrück Center for Molecular Medicine
sex or gender	male
VIAF ID	168053635
GND ID	143582119
date of birth	2000-01-01 00:00:00Z (xsd:dateTime)
family name	Heinemann
WorldCat Identities ID (superseded)	viaf-168053635
Springer Nature person ID	wds:Q28037243-E70F0928-A5FD-443C-B220-8A1E874AE91C
ORCID iD	wds:Q28037243-635A3495-8221-4C74-8F84-E6EA79831C67
Dimensions author ID	wds:Q28037243-3C6669E1-B424-4427-A3B5-C29C0B8DB44F
ORCID iD	https://orcid.org/0000-0002-8191-3850
Springer Nature person ID	01000563275.06
ORCID iD	0000-0002-8191-3850
Dimensions author ID	01000563275.06
ResearcherID	wds:Q28037243-18C25953-94F4-457F-8ACD-093E0DBD5505
Publons author ID	wds:Q28037243-6520a95a-3e1b-45aa-a1c8-1e900492a799
ResearcherID	S-3379-2016
Publons author ID	2177499
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28037243
is author of	Distinct isocomplexes of the TRAPP trafficking factor coexist inside human cells Unique self-palmitoylation activity of the transport protein particle component Bet3: a mechanism required for protein stability Structural and Biochemical Basis of Yos9 Protein Dimerization and Possible Contribution to Self-association of 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase Degradation Ubiquitin-Ligase Complex RC3H1 post-transcriptionally regulates A20 mRNA and modulates the activity of the IKK/NF-κB pathway Crystal structure of NblA from Anabaena sp. PCC 7120, a small protein playing a key role in phycobilisome degradation The SNF2-like helicase HELLS mediates E2F3-dependent transcription and cellular transformation First steps towards effective methods in exploiting high-throughput technologies for the determination of human protein structures of high biomedical value. Ribonuclease T1 with free recognition and catalytic site: crystal structure analysis at 1.5 A resolution Ribonuclease T1: Structure, Function, and Stability Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis Sequence-specific DNA binding determined by contacts outside the helix-turn-helix motif of the ParB homolog KorB. Crystallization of a Complex between Ribonuclease T1 and 2'-Guanylic Acid

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