A Catalytic Coiled Coil: Structural Insights into the Activation of the Rab GTPase Sec4p by Sec2p (Q27643770)

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English	A Catalytic Coiled Coil: Structural Insights into the Activation of the Rab GTPase Sec4p by Sec2p	scientific article

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instance of

scholarly article

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title

A Catalytic Coiled Coil: Structural Insights into the Activation of the Rab GTPase Sec4p by Sec2p (English)

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main subject

cell biology

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author

Gang Dong

object named as

Gang Dong

series ordinal

1

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author name string

Martina Medkova

series ordinal

2

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Peter Novick

series ordinal

3

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Karin M Reinisch

series ordinal

4

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publication date

9 February 2007

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published in

Molecular Cell

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volume

25

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issue

3

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page(s)

455-62

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cites work

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Structural basis of family-wide Rab GTPase recognition by rabenosyn-5

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Structural basis of Rab5-Rabaptin5 interaction in endocytosis

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A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport

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Structural basis for the selective activation of Rho GTPases by Dbl exchange factors

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Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1)

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Crystal structures of a Rab protein in its inactive and active conformations

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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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The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution

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Substructure solution with SHELXD

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Rab proteins as membrane organizers

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p

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Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to secretory vesicles; evidence for a Rab cascade in yeast

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The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis

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Interactions of Nucleotide Release Factor Dss4p with Sec4p in the Post-Golgi Secretory Pathway of Yeast

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Structural determinants of RhoA binding and nucleotide exchange in leukemia-associated Rho guanine-nucleotide exchange factor

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GRAB: a physiologic guanine nucleotide exchange factor for Rab3A, which interacts with inositol hexakisphosphate kinase

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Rabs and their effectors: achieving specificity in membrane traffic

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Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching

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The rab exchange factor Sec2p reversibly associates with the exocyst

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The structure of alpha-helical coiled coils

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Structure, exchange determinants, and family-wide rab specificity of the tandem helical bundle and Vps9 domains of Rabex-5.

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Mss4 does not function as an exchange factor for Rab in endoplasmic reticulum to Golgi transport

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Model building and refinement practice

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A cryptic Rab1-binding site in the p115 tethering protein

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27 November 2018

Sec2 is a Highly Efficient Exchange Factor for the Rab Protein Sec4

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retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Processing of X-ray diffraction data collected in oscillation mode

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/17289591

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/17289591

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1016/J.MOLCEL.2007.01.013

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4315720

OpenCitations bibliographic resource ID

4315720

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4315720

PMC publication ID

1847580

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4315720

PubMed publication ID

17289591

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4315720

ResearchGate publication ID

6514625

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