Actin-Latrunculin A Structure and Function
Open Access
- 1 September 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (36), 28120-28127
- https://doi.org/10.1074/jbc.m004253200
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Thymosin β4 serves as a glutaminyl substrate of transglutaminase. Labeling with fluorescent dansylcadaverine does not abolish interaction with G‐actin1FEBS Letters, 1999
- Impact of Profilin on Actin-Bound Nucleotide Exchange and Actin Polymerization Dynamics,Biochemistry, 1999
- Perturbations of Functional Interactions with Myosin Induce Long-Range Allosteric and Cooperative Structural Changes in ActinBiochemistry, 1997
- Thymosin β4 Binds Actin in an Extended Conformation and Contacts both the Barbed and Pointed EndsBiochemistry, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modeMethods in Enzymology, 1997
- Tβ4 Is Not a Simple G-actin Sequestering Protein and Interacts with F-actin at High ConcentrationJournal of Biological Chemistry, 1996
- Conformational changes in subdomain I of actin induced by proteolytic cleavage within the DNase I‐binding loop: energy transfer from tryptophan to AEDANSFEBS Letters, 1996
- Inhibition of actin polymerization by latrunculin AFEBS Letters, 1987
- Conformational changes in proteins as measured by difference sedimentation studies. I. Technique for measuring small changes in sedimentation coefficientBiochemistry, 1971
- Solvent content of protein crystalsJournal of Molecular Biology, 1968