Catalytically Important Residues of E6AP Ubiquitin Ligase Identified Using Acid-Cleavable Photo-Cross-Linkers

about

Catalytically Important Residues of E6AP Ubiquitin Ligase Identified Using Acid-Cleavable Photo-Cross-Linkers

Item

http://www.wikidata.org/entity/Q35925045

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年学术文章

@wuu

2015年学术文章

@zh-cn

2015年学术文章

@zh-hans

2015年学术文章

@zh-my

2015年学术文章

@zh-sg

2015年學術文章

@yue

2015年學術文章

@zh

2015年學術文章

@zh-hant

name

Catalytically Important Residu ...... -Cleavable Photo-Cross-Linkers

@ast

Catalytically Important Residu ...... -Cleavable Photo-Cross-Linkers

@en

type

Item

label

Catalytically Important Residu ...... -Cleavable Photo-Cross-Linkers

@ast

Catalytically Important Residu ...... -Cleavable Photo-Cross-Linkers

@en

prefLabel

Catalytically Important Residu ...... -Cleavable Photo-Cross-Linkers

@ast

Catalytically Important Residu ...... -Cleavable Photo-Cross-Linkers

@en

P1476

Catalytically Important Residu ...... -Cleavable Photo-Cross-Linkers

@en

P2093

Alexander V Statsyuk

http://www.w3.org/2001/XMLSchema#string

P2860

Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase

UBE3A/E6-AP mutations cause Angelman syndrome

The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53

Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5

Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade

Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade

Identification of cross-linked peptides from complex samples.

The ubiquitin-interacting motif protein, S5a, is ubiquitinated by all types of ubiquitin ligases by a mechanism different from typical substrate recognition

Strategy for "detoxification" of a cancer-derived histone mutant based on mapping its interaction with the methyltransferase PRC2

Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation.

P304

4411-4414

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1021/ACS.BIOCHEM.5B00625

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

David T Krist

P577

2015-07-20T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

26161728

http://www.w3.org/2001/XMLSchema#string

P932

4527872

http://www.w3.org/2001/XMLSchema#string