Hongjun Liu

发表

The Structural Basis of Myosin V Processive Movement as Revealed by Electron Cryomicroscopy

N. Volkmann, D. Hanein, E. Krementsova, 2022 .

Characterization of an actin-binding site within the talin FERM domain.

R. Liddington, N. Volkmann, D. Hanein, 2004, Journal of molecular biology.

Evidence for an interaction between the SH3 domain and the N-terminal extension of the essential light chain in class II myosins.

Niels Volkmann, Dorit Hanein, N. Volkmann, 2007, Journal of molecular biology.

Three-dimensional structure of vinculin bound to actin filaments.

Niels Volkmann, Dorit Hanein, N. Volkmann, 2006, Molecular cell.

The C-terminal tail domain of metavinculin, vinculin’s splice variant, severs actin filaments

N. Volkmann, D. Hanein, Hongjun Liu, 2012, The Journal of cell biology.

αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors

Simon C Watkins, Scott D. Hansen, N. Volkmann, 2013, Molecular biology of the cell.

Molecular Basis for the Dual Function of Eps8 on Actin Dynamics: Bundling and Capping

N. Volkmann, D. Hanein, K. Rottner, 2010, PLoS biology.

Passive stiffness in Drosophila indirect flight muscle reduced by disrupting paramyosin phosphorylation, but not by embryonic myosin S2 hinge substitution.

D. Swank, G. Pollack, D. Maughan, 2006, Biophysical journal.

The structure of the C-terminal actin-binding domain of talin

Niels Volkmann, Alexandre R Gingras, Neil Bate, 2007, The EMBO journal.

Drosophila paramyosin is important for myoblast fusion and essential for myofibril formation

S. Bernstein, S. Sweeney, Michelle Mardahl-Dumesnil, 2003, The Journal of cell biology.

Pseudo-atomic models of swollen CCMV from cryo-electron microscopy data.

John E. Johnson, David A Case, Chunxu Qu, 2003, Journal of structural biology.

Paramyosin phosphorylation site disruption affects indirect flight muscle stiffness and power generation in Drosophila melanogaster.

D. Swank, D. Maughan, S. Bernstein, 2005, Proceedings of the National Academy of Sciences of the United States of America.