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Structure and mutational analysis of Rab GDP-dissociation inhibitor
scientific article
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scholarly article
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title
Structure and mutational analysis of Rab GDP-dissociation inhibitor
(English)
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main subject
mutational analysis
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based on heuristic
inferred from title
author
Enrico Stura
series ordinal
4
object named as
E A Stura
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author name string
I Schalk
series ordinal
1
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K Zeng
series ordinal
2
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S K Wu
series ordinal
3
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J Matteson
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5
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M Huang
series ordinal
6
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A Tandon
series ordinal
7
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I A Wilson
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8
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W E Balch
series ordinal
9
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language of work or name
English
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publication date
2 May 1996
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published in
Nature
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volume
381
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page(s)
42-8
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issue
6577
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cites work
Rab GDP dissociation inhibitor: putting rab GTPases in the right place.
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GTPases: multifunctional molecular switches regulating vesicular traffic
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cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein
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An autosomal homologue of the choroideremia gene colocalizes with the Usher syndrome type II locus on the distal part of chromosome 1q
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Purification of component A of Rab geranylgeranyl transferase: possible identity with the choroideremia gene product
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Retinal degeneration in choroideremia: deficiency of rab geranylgeranyl transferase
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Cloning and characterization of the human choroideremia gene
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MRS6--yeast homologue of the choroideraemia gene.
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Identification of yeast component A: reconstitution of the geranylgeranyltransferase that modifies Ypt1p and Sec4p
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Structure and mechanism of para-hydroxybenzoate hydroxylase.
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Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 A resolution
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Crystal structure of cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases
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Protein structure comparison by alignment of distance matrices
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Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 A resolution. Analysis of the enzyme-substrate and enzyme-product complexes
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Crystal structure of p-hydroxybenzoate hydroxylase
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Prediction of the occurrence of the ADP-binding beta alpha beta-fold in proteins, using an amino acid sequence fingerprint
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Guanine nucleotide dissociation inhibitor is essential for Rab1 function in budding from the endoplasmic reticulum and transport through the Golgi stack
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Rab GDI: a solubilizing and recycling factor for rab9 protein
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Membrane association of Rab5 mediated by GDP-dissociation inhibitor and accompanied by GDP/GTP exchange
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The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue
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The 2.0 A crystal structure of a heterotrimeric G protein
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The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2
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Crystallization and preliminary crystallographic data for Rab guanine nucleotide dissociation inhibitor (RabGDI) from bovine brain
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Solvent content of protein crystals
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Resolution of phase ambiguity in macromolecular crystallography
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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
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PROCHECK: a program to check the stereochemical quality of protein structures
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
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A GDP-bound of rab1 inhibits protein export from the endoplasmic reticulum and transport between Golgi compartments
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Purification of His6-tagged Rab1 proteins using bacterial and insect cell expression systems
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Quantitative analysis of the interactions between prenyl Rab9, GDP dissociation inhibitor-alpha, and guanine nucleotides
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A small GTP-binding protein dissociates from synaptic vesicles during exocytosis.
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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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Identifiers
DOI
10.1038/381042A0
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2578891
Dimensions Publication ID
1037727376
0 references
OpenCitations bibliographic resource ID
2578891
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2578891
PubMed ID
8609986
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2578891
Springer Nature article ID
10.1038/381042a0
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