Structural basis of the phosphorylation-independent recognition of cydin D1 by the SCFFBXO31 ubiquitin ligase
Journal Article
Overview
publication date
- January 9, 2018
has subject area
- Biochemical Phenomena - Amino Acid Sequence
- Biochemical Phenomena - Phosphorylation
- Biochemical Phenomena - Protein Binding
- Biochemical Phenomena - Proteolysis
- Biochemical Phenomena - Sequence Homology, Amino Acid
- Biochemical Phenomena - Ubiquitination
- Biochemical Phenomena - Ubiquitination
- Cell Cycle Proteins - Cyclin D1
- Cell Line - HeLa Cells
- Crystallography, X-Ray
- Epithelial Cells - HeLa Cells
- F-Box Proteins
- Gene Expression Regulation - Ubiquitination
- Genetic Phenomena - Sequence Homology, Amino Acid
- Humans
- Metabolism - Phosphorylation
- Metabolism - Protein Binding
- Metabolism - Proteolysis
- Metabolism - Ubiquitination
- Models, Molecular
- Molecular Sequence Data - Amino Acid Sequence
- Multiprotein Complexes
- Organic Chemistry Phenomena - Phosphorylation
- Peptides - Cyclin D1
- Protein Structural Elements - Protein Domains
- Protein Structure, Tertiary - Protein Domains
- Proteins - Cyclin D1
- Proto-Oncogene Proteins - Cyclin D1
- Substrate Specificity
- Tumor Cells, Cultured - HeLa Cells
- Tumor Suppressor Proteins
has restriction
- bronze
Date in CU Experts
- January 5, 2018 12:30 PM
Full Author List
- Li Y; Jin K; Bunker E; Zhang X; Luo X; Liu X; Hao B
author count
- 7
citation count
- 39
published in
Other Profiles
International Standard Serial Number (ISSN)
- 0027-8424
Digital Object Identifier (DOI)
Additional Document Info
start page
- 319
end page
- 324
volume
- 115
issue
- 2