MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes

Molecular Cell

Volumn 63, Issue 1, 2016, Pages 146-155

  Abdul Rehman, Syed Arif ^a   Kristariyanto, Yosua Adi ^a   Choi, Soo Youn ^a   Nkosi, Pedro Junior ^a   Weidlich, Simone ^a   Labib, Karim ^a   Hofmann, Kay ^b   Kulathu, Yogesh ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

^b UNIVERSITY OF COLOGNE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

DEUBIQUITINASE; MINDY PROTEIN; POLYUBIQUITIN; UNCLASSIFIED DRUG; FAM188A PROTEIN, HUMAN; FAM18B PROTEIN, HUMAN; FAM63B PROTEIN, HUMAN; MEMBRANE PROTEIN; MINDY-1 PROTEIN, HUMAN; NUCLEAR PROTEIN; TUMOR SUPPRESSOR PROTEIN; UBIQUITIN THIOLESTERASE;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME STRUCTURE; GENETIC CODE; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN HOMEOSTASIS; AMINO ACID SEQUENCE; CHEMISTRY; CONSERVED SEQUENCE; ENZYME SPECIFICITY; HUMAN; METABOLISM; MOLECULAR EVOLUTION; MOLECULAR MODEL; PROTEIN FOLDING; STRUCTURE ACTIVITY RELATION; UBIQUITINATION;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CONSERVED SEQUENCE; DEUBIQUITINATING ENZYMES; EVOLUTION, MOLECULAR; HUMANS; MEMBRANE PROTEINS; MODELS, MOLECULAR; NUCLEAR PROTEINS; POLYUBIQUITIN; PROTEIN FOLDING; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TUMOR SUPPRESSOR PROTEINS; UBIQUITIN THIOLESTERASE; UBIQUITINATION;

EID: 84992409187     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2016.05.009     Document Type: Article

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