Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases (Q27626747)

https://doi.org/10.1016%2FS0092-8674%2800%2900057-X

14 April 2017

author name string

Ning Zheng

1

1 reference

https://doi.org/10.1016%2FS0092-8674%2800%2900057-X

14 April 2017

Ping Wang

2

1 reference

https://doi.org/10.1016%2FS0092-8674%2800%2900057-X

14 April 2017

Philip D. Jeffrey

3

1 reference

https://doi.org/10.1016%2FS0092-8674%2800%2900057-X

14 April 2017

Nikola P. Pavletich

4

1 reference

https://doi.org/10.1016%2FS0092-8674%2800%2900057-X

14 April 2017

publication date

August 2000

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https://doi.org/10.1016%2FS0092-8674%2800%2900057-X

14 April 2017

language of work or name

0 references

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https://doi.org/10.1016%2FS0092-8674%2800%2900057-X

14 April 2017

volume

102

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https://doi.org/10.1016%2FS0092-8674%2800%2900057-X

14 April 2017

issue

4

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https://doi.org/10.1016%2FS0092-8674%2800%2900057-X

14 April 2017

page(s)

533-539

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Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster

14 April 2017

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Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53

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D-Cbl, the Drosophila homologue of the c-Cbl proto-oncogene, interacts with the Drosophila EGF receptor in vivo, despite lacking C-terminal adaptor binding sites.

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

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7 January 2021

The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase

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Improved methods for building protein models in electron density maps and the location of errors in these models

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The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2

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How the cyclin became a cyclin: regulated proteolysis in the cell cycle

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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Substrate targeting in the ubiquitin system

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The Cbl protooncoprotein stimulates CSF-1 receptor multiubiquitination and endocytosis, and attenuates macrophage proliferation

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Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1

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The Cbl phosphotyrosine-binding domain selects a D(N/D)XpY motif and binds to the Tyr292 negative regulatory phosphorylation site of ZAP-70.

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Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase

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Raster3D: photorealistic molecular graphics

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The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor alpha

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity

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7 January 2021

The product of the proto-oncogene c-cbl: a negative regulator of the Syk tyrosine kinase

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The RING Finger Domain of Cbl Is Essential for Negative Regulation of the Syk Tyrosine Kinase

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7 January 2021

Processing of X-ray diffraction data collected in oscillation mode

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

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Characterization of Human hect Domain Family Members and Their Interaction with UbcH5 and UbcH7

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Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1.

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7 January 2021

Degradation signals in the lysine-asparagine sequence space

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The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain

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Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli

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Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7

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Identification of a Cullin Homology Region in a Subunit of the Anaphase-Promoting Complex

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Mass spectrometric analysis of the anaphase-promoting complex from yeast: identification of a subunit related to cullins.

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Identifiers

DOI

2 references

https://doi.org/10.1016%2FS0092-8674%2800%2900057-X

14 April 2017

Consolidated OpenCitations Corpus – April 2017

2112088

Consolidated OpenCitations Corpus – April 2017

2 references

2112088

PubMed publication ID

10966114

1 reference

Consolidated OpenCitations Corpus – April 2017