Ubiquitination independent of E1 and E2 enzymes by bacterial effectors

Nature

Volumn 533, Issue 7601, 2016, Pages 120-124

  Qiu, Jiazhang ^a   Sheedlo, Michael J ^b   Yu, Kaiwen ^c   Tan, Yunhao ^a,e   Nakayasu, Ernesto S ^d   Das, Chittaranjan ^b   Liu, Xiaoyun ^c   Luo, Zhao Qing ^a  

^a PURDUE UNIVERSITY   (United States)

^b PURDUE UNIVERSITY   (United States)

^c PEKING UNIVERSITY   (China)

^d PACIFIC NORTHWEST NATIONAL LABORATORY   (United States)

^e BOSTON CHILDREN S HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; SIDE EFFECTOR FAMILY PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E1; UBIQUITIN PROTEIN LIGASE E2; UNCLASSIFIED DRUG; ADENOSINE DIPHOSPHATE RIBOSE; ADENOSINE TRIPHOSPHATE; MEMBRANE PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; RAB PROTEIN; SDEA PROTEIN, LEGIONELLA PNEUMOPHILA; UBIQUITIN CONJUGATING ENZYME; VIRULENCE FACTOR;

AMINO ACID; BACTERIUM; CATALYSIS; ENZYME ACTIVITY; EUKARYOTE; IMMUNE RESPONSE; IMMUNE SYSTEM; PATHOGENICITY; PHYSIOLOGICAL RESPONSE; PROTEIN; VIRULENCE;

ADENOSINE DIPHOSPHATE RIBOSYLATION; ARTICLE; BACTERIAL GROWTH; CATALYSIS; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; IN VITRO STUDY; LEGIONELLA PNEUMOPHILA; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN MOTIF; UBIQUITINATION; AMINO ACID SEQUENCE; BACTERIAL LOAD; BIOCATALYSIS; CHEMISTRY; CYTOLOGY; ENZYMOLOGY; METABOLISM; MOLECULAR GENETICS; PATHOGENICITY;

BACTERIA (MICROORGANISMS); EUKARYOTA; LEGIONELLA PNEUMOPHILA; PROTOZOA;

ADENOSINE DIPHOSPHATE RIBOSE; ADENOSINE TRIPHOSPHATE; ADP RIBOSE TRANSFERASES; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL LOAD; BACTERIAL PROTEINS; BIOCATALYSIS; ENDOPLASMIC RETICULUM; LEGIONELLA PNEUMOPHILA; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; NAD; RAB GTP-BINDING PROTEINS; UBIQUITIN; UBIQUITIN-ACTIVATING ENZYMES; UBIQUITIN-CONJUGATING ENZYMES; UBIQUITINATION; VIRULENCE FACTORS;

EID: 84966350690     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature17657     Document Type: Article

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