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TBC1D16 is a Rab4A GTPase activating protein that regulates receptor recycling and EGF receptor signaling
scientific journal article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
23019362
retrieved
4 January 2017
title
TBC1D16 is a Rab4A GTPase activating protein that regulates receptor recycling and EGF receptor signaling
(English)
1 reference
stated in
PubMed
PubMed ID
23019362
retrieved
4 January 2017
main subject
TBC1 domain family member 16
1 reference
stated in
GOA release 2020-03-11
author name string
Basem S. Goueli
series ordinal
1
author given names
Basem S
author last names
Goueli
1 reference
stated in
PubMed
PubMed ID
23019362
retrieved
4 January 2017
Marianne Broome Powell
series ordinal
2
author given names
Marianne Broome
author last names
Powell
1 reference
stated in
PubMed
PubMed ID
23019362
retrieved
4 January 2017
Elizabeth C. Finger
series ordinal
3
author given names
Elizabeth C
author last names
Finger
1 reference
stated in
PubMed
PubMed ID
23019362
retrieved
4 January 2017
Suzanne R. Pfeffer
series ordinal
4
author given names
Suzanne R
author last names
Pfeffer
1 reference
stated in
PubMed
PubMed ID
23019362
retrieved
4 January 2017
language of work or name
English
0 references
publication date
25 September 2012
1 reference
stated in
PubMed
PubMed ID
23019362
retrieved
4 January 2017
published in
Proceedings of the National Academy of Sciences of the United States of America
1 reference
stated in
PubMed
PubMed ID
23019362
retrieved
4 January 2017
volume
109
1 reference
stated in
PubMed
PubMed ID
23019362
retrieved
4 January 2017
issue
39
1 reference
stated in
PubMed
PubMed ID
23019362
retrieved
4 January 2017
page(s)
15787–15792
1 reference
stated in
PubMed
PubMed ID
23019362
retrieved
4 January 2017
describes a project that uses
ImageJ
1 reference
stated in
Europe PubMed Central
retrieved
11 June 2022
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3465424/fullTextXML
based on heuristic
inferred from PubMed Central ID database lookup
cites work
Rab35 regulates an endocytic recycling pathway essential for the terminal steps of cytokinesis
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PubMed Central
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Specific Rab GTPase-activating proteins define the Shiga toxin and epidermal growth factor uptake pathways
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A role for the small GTPase Rab21 in the early endocytic pathway
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RUTBC1 protein, a Rab9A effector that activates GTP hydrolysis by Rab32 and Rab33B proteins
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Functional dissection of Rab GTPases involved in primary cilium formation
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Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer
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Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells
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20 March 2017
TIP47 is a key effector for Rab9 localization
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Analysis of the eukaryotic prenylome by isoprenoid affinity tagging
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Rab GTPases as coordinators of vesicle traffic
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Novel MITF targets identified using a two-step DNA microarray strategy
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Rab17 regulates membrane trafficking through apical recycling endosomes in polarized epithelial cells
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The small GTP-binding protein rab4 controls an early sorting event on the endocytic pathway
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TBC proteins: GAPs for mammalian small GTPase Rab?
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Regulation of exosome secretion by Rab35 and its GTPase-activating proteins TBC1D10A-C.
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VEGF-A-stimulated signalling in endothelial cells via a dual receptor tyrosine kinase system is dependent on co-ordinated trafficking and proteolysis
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TBC1D20 is a Rab1 GTPase-activating protein that mediates hepatitis C virus replication
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TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.
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Targeting Rab GTPases to distinct membrane compartments
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Segregation of transferrin to a mildly acidic (pH 6.5) para-Golgi compartment in the recycling pathway
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Activation of protein kinase C alpha is necessary for sorting the PDGF beta-receptor to Rab4a-dependent recycling
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2 June 2018
Endocytosis and intracellular trafficking of ErbBs
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VEGF regulates the mobilization of VEGFR2/KDR from an intracellular endothelial storage compartment
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Identifiers
DOI
10.1073/PNAS.1204540109
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1404565
ADS bibcode
2012PNAS..10915787G
0 references
OpenCitations bibliographic resource ID
1404565
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1404565
PMCID
3465424
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1404565
PubMed ID
23019362
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1404565
ResearchGate publication ID
231225493
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