Backbone 1H, 13C, and 15N assignments of yeast Ump1, an intrinsically disordered protein that functions as a proteasome assembly chaperone

Biomolecular NMR Assignments

Volumn 8, Issue 2, 2014, Pages 383-386

  Uekusa, Yoshinori ^a,b   Okawa, Keisuke ^a   Yagi Utsumi, Maho ^a,b,c   Serve, Olivier ^b   Nakagawa, Yuki ^a   Mizushima, Tsunehiro ^a,d   Yagi, Hirokazu ^a   Saeki, Yasushi ^e   Tanaka, Keiji ^e   Kato, Koichi ^a,b  

^a NAGOYA CITY UNIVERSITY   (Japan)

^b OKAZAKI INSTITUTE FOR INTEGRATIVE BIOSCIENCE   (Japan)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^d UNIVERSITY OF HYOGO   (Japan)

^e TOKYO METROPOLITAN INSTITUTE OF MEDICAL SCIENCE   (Japan)

Author keywords

Intrinsically unstructured protein; NMR spectroscopy; Proteasome assembly; Resonance assignment; Ump1

Indexed keywords

CHAPERONE; INTRINSICALLY DISORDERED PROTEIN; PROTEASOME; PROTEASOME MATURATION PROTEIN;

CHEMISTRY; METABOLISM; NUCLEAR MAGNETIC RESONANCE; SACCHAROMYCES CEREVISIAE;

INTRINSICALLY DISORDERED PROTEINS; MOLECULAR CHAPERONES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEASOME ENDOPEPTIDASE COMPLEX; SACCHAROMYCES CEREVISIAE;

EID: 84889973482     PISSN: 18742718     EISSN: 1874270X     Source Type: Journal    
DOI: 10.1007/s12104-013-9523-1     Document Type: Article

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