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Structural basis of family-wide Rab GTPase recognition by rabenosyn-5
scientific article
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scholarly article
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title
Structural basis of family-wide Rab GTPase recognition by rabenosyn-5
(English)
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main subject
RAB14, member RAS oncogene family
1 reference
stated in
GOA release 2020-03-11
RAB4A, member RAS oncogene family
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stated in
GOA release 2020-03-11
RAB2A, member RAS oncogene family
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stated in
GOA release 2020-03-11
RAB21, member RAS oncogene family
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stated in
GOA release 2020-03-11
GDP binding
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stated in
GOA release 2020-03-11
RAB22A, member RAS oncogene family
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stated in
GOA release 2020-03-11
author name string
Sudharshan Eathiraj
series ordinal
1
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Xiaojing Pan
series ordinal
2
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Christopher Ritacco
series ordinal
3
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David G Lambright
series ordinal
4
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language of work or name
English
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publication date
21 July 2005
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published in
Nature
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volume
436
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issue
7049
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page(s)
415-9
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cites work
A role for the small GTPase Rab21 in the early endocytic pathway
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Structural basis of Rab5-Rabaptin5 interaction in endocytosis
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19 March 2017
Structure of the Rab7:REP-1 complex: insights into the mechanism of Rab prenylation and choroideremia disease
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Rab14 is involved in membrane trafficking between the Golgi complex and endosomes
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19 March 2017
rabip4′ Is an Effector of rab5 and rab4 and Regulates Transport through Early Endosomes
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19 March 2017
Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus
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The small GTPase Rab22 interacts with EEA1 and controls endosomal membrane trafficking
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Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5
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PubMed Central
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Molecular cloning of two novel rab genes from human melanocytes
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Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments
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19 March 2017
Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase
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19 March 2017
Structural plasticity of an invariant hydrophobic triad in the switch regions of Rab GTPases is a determinant of effector recognition
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19 March 2017
Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A
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Rab proteins as membrane organizers
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19 March 2017
Dual prenylation is required for Rab protein localization and function
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PubMed Central
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19 March 2017
The guanine nucleotide-binding switch in three dimensions
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19 March 2017
Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2
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PubMed Central
reference URL
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19 March 2017
Evolution of the Rab family of small GTP-binding proteins
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19 March 2017
Role of rRAB22b, an oligodendrocyte protein, in regulation of transport of vesicles from trans Golgi to endocytic compartments
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PubMed Central
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19 March 2017
Rab9 functions in transport between late endosomes and the trans Golgi network
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PubMed Central
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19 March 2017
Rab GTPases: specifying and deciphering organelle identity and function
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7 April 2017
Structural clues to Rab GTPase functional diversity
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PubMed Central
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27 September 2017
Targeting Rab GTPases to distinct membrane compartments
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PubMed Central
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27 September 2017
Controlling the location and activation of Rab GTPases
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PubMed Central
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27 September 2017
Yip3 catalyses the dissociation of endosomal Rab–GDI complexes
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PubMed Central
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27 September 2017
Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes.
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PubMed Central
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27 September 2017
Rab 7: an important regulator of late endocytic membrane traffic
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PubMed Central
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27 September 2017
Switch-of-Function Mutants Based on Morphology Classification of Ras Superfamily Small GTPases
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PubMed Central
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30 May 2018
Rab22a affects the morphology and function of the endocytic pathway.
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PubMed Central
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29 November 2018
The mammalian Rab family of small GTPases: definition of family and subfamily sequence motifs suggests a mechanism for functional specificity in the Ras superfamily.
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1360218
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29 November 2018
Identifiers
DOI
10.1038/NATURE03798
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2391147
Dimensions Publication ID
1008748952
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Fatcat ID
release_v7n6jxbhpjfetjgcjf2so4odti
0 references
OpenCitations bibliographic resource ID
2391147
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2391147
PMC publication ID
1360218
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2391147
PubMed publication ID
16034420
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2391147
ResearchGate publication ID
7711683
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