Thermodynamics of the Op18/stathmin-tubulin interaction (Q28910365)

7 March 2017

title

Thermodynamics of the Op18/stathmin-tubulin interaction (English)

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regulation of microtubule polymerization or depolymerization

7 March 2017

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GOA release 2020-03-11

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GOA release 2020-03-11

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Michel O. Steinmetz

5

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author name string

Srinivas Honnappa

1

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7 March 2017

Brian Cutting

2

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7 March 2017

Wolfgang Jahnke

3

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7 March 2017

Joachim Seelig

4

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7 March 2017

language of work or name

English

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publication date

3 October 2003

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Journal of Biological Chemistry

7 March 2017

published in

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7 March 2017

volume

278

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7 March 2017

issue

40

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7 March 2017

page(s)

38926–38934

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Dynamic instability of microtubule growth

7 March 2017

cites work

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Microtubule dynamics: if you need a shrink try stathmin/Op18.

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Overexpression of the stathmin gene in a subset of human breast cancer

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Op18/stathmin caps a kinked protofilament-like tubulin tetramer

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Isotope-tagged cross-linking reagents. A new tool in mass spectrometric protein interaction analysis

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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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Phosphorylation disrupts the central helix in Op18/stathmin and suppresses binding to tubulin

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Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules

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Stathmin: a tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules

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Distinct roles of PP1 and PP2A-like phosphatases in control of microtubule dynamics during mitosis

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Op18/stathmin mediates multiple region-specific tubulin and microtubule-regulating activities

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Structural transitions at microtubule ends correlate with their dynamic properties in Xenopus egg extracts

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The catastrophe-promoting activity of ectopic Op18/stathmin is required for disruption of mitotic spindles but not interphase microtubules

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Autonomous and phosphorylation-responsive microtubule-regulating activities of the N-terminus of Op18/stathmin.

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The effect of stathmin phosphorylation on microtubule assembly depends on tubulin critical concentration

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Stathmin family proteins display specific molecular and tubulin binding properties

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High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli.

21 January 2018

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Heteronuclear NMR assignments and secondary structure of the coiled coil trimerization domain from cartilage matrix protein in oxidized and reduced forms

21 January 2018

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GDP state of tubulin: stabilization of double rings

21 January 2018

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Rapid measurement of binding constants and heats of binding using a new titration calorimeter

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Titration calorimetry of lipid-peptide interactions

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Mutations of oncoprotein 18/stathmin identify tubulin-directed regulatory activities distinct from tubulin association

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Molecular dissection of GTP exchange and hydrolysis within the ternary complex of tubulin heterodimers and Op18/stathmin family members

21 January 2018

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Prediction of binding energetics from structure using empirical parameterization

21 January 2018

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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

21 January 2018

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Microtubule structure at improved resolution

21 January 2018

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High-resolution model of the microtubule

21 January 2018

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Stathmin: a relay phosphoprotein for multiple signal transduction?

21 January 2018

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Quantitative analysis of Op18 phosphorylation in childhood acute leukemia

21 January 2018

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Stathmin slows down guanosine diphosphate dissociation from tubulin in a phosphorylation-controlled fashion

21 January 2018

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Preparation of single molecules and supramolecular complexes for high-resolution metal shadowing

21 January 2018

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Mutational analysis of op18/stathmin-tubulin-interacting surfaces. Binding cooperativity controls tubulin GTP hydrolysis in the ternary complex

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M305546200

1 reference

Consolidated OpenCitations Corpus – April 2017

release_ga74jd2qmrbkbnumtmtiynmlna

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/ga74jd2qmrbkbnumtmtiynmlna

mapped directly with Wikidata item

24 November 2022

based on heuristic

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017