E. Ballweber

发表

Polymerisation of chemically cross-linked actin:thymosin beta(4) complex to filamentous actin: alteration in helical parameters and visualisation of thymosin beta(4) binding on F-actin.

H. Mannherz, U. Aebi, D. Stoffler, 2002, Journal of molecular biology.

Nuclear localisation of the G-actin sequestering peptide thymosin β4

H. Mannherz, A. Otto, E. Hannappel, 2004, Journal of Cell Science.

Thymosin β4 serves as a glutaminyl substrate of transglutaminase. Labeling with fluorescent dansylcadaverine does not abolish interaction with G‐actin 1

H. Mannherz, T. Bonk, A. Humeny, 1999 .

Interaction of isolated cross‐linked short actin oligomers with the skeletal muscle myosin motor domain

H. Mannherz, C. Herrmann, R. Schröder, 2018, The FEBS journal.

Induction of the polymerization of actin from the actin:thymosin beta 4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin.

H. Mannherz, E. Hannappel, B. Niggemeyer, 1994, European journal of biochemistry.

Mapping the ADF/cofilin binding site on monomeric actin by competitive cross-linking and peptide array: evidence for a second binding site on monomeric actin.

H. Mannherz, C. Granier, C. Steegborn, 2007, Journal of molecular biology.

Cross-linked long-pitch actin dimer forms stoichiometric complexes with gelsolin segment 1 and/or deoxyribonuclease I that nonproductively interact with myosin subfragment 1.

R. Goody, H. Mannherz, G. Hegyi, 2008, Biochemistry.

Mapping the binding site of thymosin beta4 on actin by competition with G-actin binding proteins indicates negative co-operativity between binding sites located on opposite subdomains of actin.

H. Mannherz, E. Hannappel, T. Huff, 1997, The Biochemical journal.

Thymosin beta(4) serves as a glutaminyl substrate of transglutaminase. Labeling with fluorescent dansylcadaverine does not abolish interaction with G-actin.

H. Mannherz, T. Bonk, A. Humeny, 1999, FEBS letters.

Plant profilin induces actin polymerization from actin:β‐thymosin complexes and competes directly with β‐thymosins and with negative co‐operativity with DNase I for binding to actin

H. Mannherz, B. Jockusch, E. Hannappel, 1998, FEBS letters.