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The 4 A X-ray structure of a tubulin:stathmin-like domain complex
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title
The 4 A X-ray structure of a tubulin:stathmin-like domain complex
(English)
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author name string
B Gigant
series ordinal
1
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P A Curmi
series ordinal
2
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C Martin-Barbey
series ordinal
3
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E Charbaut
series ordinal
4
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S Lachkar
series ordinal
5
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L Lebeau
series ordinal
6
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S Siavoshian
series ordinal
7
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A Sobel
series ordinal
8
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M Knossow
series ordinal
9
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language of work or name
English
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publication date
15 September 2000
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published in
Cell
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volume
102
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page(s)
809-16
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issue
6
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cites work
Methods used in the structure determination of bovine mitochondrial F1 ATPase
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The free energy for hydrolysis of a microtubule-bound nucleotide triphosphate is near zero: all of the free energy for hydrolysis is stored in the microtubule lattice
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Molecular characterization of human stathmin expressed in Escherichia coli: site-directed mutagenesis of two phosphorylatable serines (Ser-25 and Ser-63)
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Solution structure of GDP-tubulin double rings to 3 nm resolution and comparison with microtubules
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Phosphorylation regulates the microtubule-destabilizing activity of stathmin and its interaction with tubulin.
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Stathmin: a tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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Mutations of oncoprotein 18/stathmin identify tubulin-directed regulatory activities distinct from tubulin association
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A single amino acid difference distinguishes the human and the rat sequences of stathmin, a ubiquitous intracellular phosphoprotein associated with cell regulations
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Regulation of microtubule dynamics by Ca2+/calmodulin-dependent kinase IV/Gr-dependent phosphorylation of oncoprotein 18
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Cold depolymerization of microtubules to double rings: geometric stabilization of assemblies
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Dynamic instability of microtubule growth
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Structural changes at microtubule ends accompanying GTP hydrolysis: information from a slowly hydrolyzable analogue of GTP, guanylyl (alpha,beta)methylenediphosphonate
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AMoRe: an automated package for molecular replacement
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Structure of the alpha beta tubulin dimer by electron crystallography
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The stathmin family -- molecular and biological characterization of novel mammalian proteins expressed in the nervous system.
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Probing the native structure of stathmin and its interaction domains with tubulin. Combined use of limited proteolysis, size exclusion chromatography, and mass spectrometry.
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Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinement
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Regulation of microtubule dynamics by the neuronal growth-associated protein SCG10.
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Stathmin: a relay phosphoprotein for multiple signal transduction?
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Op18/stathmin caps a kinked protofilament-like tubulin tetramer
1 reference
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1 reference
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Identifiers
DOI
10.1016/S0092-8674(00)00069-6
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
991760
OpenCitations bibliographic resource ID
991760
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
991760
PubMed ID
11030624
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
991760
ResearchGate publication ID
262032390
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