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Rab1A is an mTORC1 activator and a colorectal oncogene
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scholarly article
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title
Rab1A is an mTORC1 activator and a colorectal oncogene
(English)
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main subject
cell biology
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author name string
Janice D Thomas
series ordinal
1
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Yan-Jie Zhang
series ordinal
2
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Yue-Hua Wei
series ordinal
3
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Jun-Hung Cho
series ordinal
4
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Laura E Morris
series ordinal
5
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Hui-Yun Wang
series ordinal
6
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X F Steven Zheng
series ordinal
7
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language of work or name
English
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publication date
10 November 2014
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published in
Cancer Cell
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volume
26
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page(s)
754-69
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issue
5
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cites work
A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1
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Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway
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Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
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The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1
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PubMed Central
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The RAB25 small GTPase determines aggressiveness of ovarian and breast cancers
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Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton
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Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
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Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control
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19 March 2017
Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B
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Leucyl-tRNA synthetase controls TORC1 via the EGO complex
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PubMed Central
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The Vam6 GEF controls TORC1 by activating the EGO complex
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Dual prenylation is required for Rab protein localization and function
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19 March 2017
Functional discovery via a compendium of expression profiles
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19 March 2017
The 14-3-3 proteins positively regulate rapamycin-sensitive signaling
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19 March 2017
Rab GTPases as coordinators of vesicle traffic
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19 March 2017
The mammalian target of rapamycin (mTOR) pathway regulates mitochondrial oxygen consumption and oxidative capacity
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19 March 2017
Localization of Rheb to the endomembrane is critical for its signaling function
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Rab GTPases Are Recruited to Chlamydial Inclusions in Both a Species-Dependent and Species-Independent Manner
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19 March 2017
Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins
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19 March 2017
Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb
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19 March 2017
Role of Rab GTPases in membrane traffic and cell physiology
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7 April 2017
Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress
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7 April 2017
Regulation of TORC1 by Rag GTPases in nutrient response
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7 April 2017
Direct observation of individual endogenous protein complexes in situ by proximity ligation
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The TOR pathway: a target for cancer therapy
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mTOR direct interactions with Rheb-GTPase and raptor: sub-cellular localization using fluorescence lifetime imaging
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The TOR complex 1 is a direct target of Rho1 GTPase
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27 September 2017
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27 September 2017
Regulation of mTORC1 by the Rab and Arf GTPases
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27 September 2017
Differential requirement of CAAX-mediated posttranslational processing for Rheb localization and signaling
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27 September 2017
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27 September 2017
COPI recruitment is modulated by a Rab1b-dependent mechanism
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27 September 2017
Membrane targeting of Rab GTPases is influenced by the prenylation motif
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27 September 2017
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27 September 2017
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27 September 2017
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Inhibition of mTOR signaling with rapamycin regresses established cardiac hypertrophy induced by pressure overload
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FKBP12-Rapamycin-associated Protein or Mammalian Target of Rapamycin (FRAP/mTOR) Localization in the Endoplasmic Reticulum and the Golgi Apparatus
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Increased myocardial Rab GTPase expression: a consequence and cause of cardiomyopathy
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1016/J.CCELL.2014.09.008
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
789552
OpenCitations bibliographic resource ID
789552
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
789552
PMCID
4288827
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
789552
PubMed ID
25446900
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
789552
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