Structural Mass Spectrometry of the αβ-Tubulin Dimer Supports a Revised Model of Microtubule Assembly-Reference-Cited by-同舟云学术

Structural Mass Spectrometry of the αβ-Tubulin Dimer Supports a Revised Model of Microtubule Assembly

Published:2009-05-04 Issue:22 Volume:48 Page:4858-4870
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Bennett Melissa J.¹,Chik John. K.¹,Slysz Gordon W.¹,Luchko Tyler²,Tuszynski Jack²,Sackett Dan L.³,Schriemer David C.¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, University of Calgary, 3330 Hospital Drive NW, Calgary, Alberta, Canada T2N 4N1

2. Division of Experimental Oncology, Cross Cancer Institute, 11560 University Avenue, Edmonton, Alberta, Canada T6G 1Z2

3. Eunice Kennedy Shriver National Institute of Child Health and Human Development, Laboratory of Integrative and Medical Biophysics, National Institutes of Health, 9 Memorial Drive, Bethesda, Maryland 20892-0924

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi900200q

Reference48 articles.

1. MICROTUBULE POLYMERIZATION DYNAMICS

2. Control of the Structural Stability of the Tubulin Dimer by One High Affinity Bound Magnesium Ion at Nucleotide N-site

3. Dissociation of the Tubulin Dimer Is Extremely Slow, Thermodynamically Very Unfavorable, and Reversible in the Absence of an Energy Source

4. Refined structure of αβ-tubulin at 3.5 Å resolution 1 1Edited by I. A. Wilson

5. Kinetic analysis of guanosine 5'-triphosphate hydrolysis associated with tubulin polymerization

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