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The cullin-RING ubiquitin-protein ligases
Zhihua Hua
, Richard D. Vierstra
Department of Biology
Roy and Diana Vagelos Division of Biology & Biomedical Sciences (DBBS)
DBBS - Molecular Cell Biology
DBBS - Plant and Microbial Biosciences
DBBS - Biochemistry, Biophysics, and Structural Biology
Research output
:
Contribution to journal
›
Article
›
peer-review
440
Scopus citations
Overview
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Keyphrases
Ubiquitin Ligase
100%
Cullin-RING Ligase
100%
Cullin-RING
100%
Ubiquitin
75%
Signaling Pathway
25%
Stress Response
25%
Genetic Studies
25%
Polypeptide
25%
Adaptor
25%
Genomic Studies
25%
Post-translational
25%
Housekeeping
25%
Highly Polymorphic
25%
Primary Function
25%
Regulatory Role
25%
Ubiquitylation
25%
Plant Biology
25%
Evolutionary History
25%
26S Proteasome
25%
Ubiquitin Conjugation
25%
Plant Protein
25%
Organizational Complexity
25%
Pathogen Defense
25%
Self-incompatibility
25%
Plant Lineages
25%
Cullin
25%
Substrate Potential
25%
Dynamic Substrate
25%
Biochemistry, Genetics and Molecular Biology
Ubiquitin-Conjugating Enzyme
100%
Cullin
100%
Ubiquitin
66%
Ligase
66%
Genetics
16%
Dynamics
16%
Cell Cycle
16%
Infectious Agent
16%
Transcription
16%
Proteasome
16%
Ubiquitination
16%
Self Incompatibility
16%
Genomics
16%
Pharmacology, Toxicology and Pharmaceutical Science
Ubiquitin Protein Ligase
100%
Cullin
100%
Ligase
66%
Ubiquitin
66%
Proteasome
16%
Polypeptide
16%
Infectious Agent
16%
Plant Protein
16%
Immunology and Microbiology
Ubiquitins
100%
Infectious Agent
16%
Cell Cycle
16%
Lineages
16%
Ubiquitination
16%
Proteasome
16%
Dynamics
16%
Self Incompatibility
16%
Vertebral Column
16%