His primary areas of investigation include Actin, Biochemistry, Actin-binding protein, Myosin and Cell biology. Emil Reisler combines subjects such as Protein filament, Cysteine, Cytoskeleton, Protein structure and Binding site with his study of Actin. His research on Biochemistry frequently connects to adjacent areas such as Biophysics.
Many of his studies on Actin-binding protein involve topics that are commonly interrelated, such as Arp2/3 complex. His studies in Myosin integrate themes in fields like ATPase, Adenosine triphosphatase and Subtilisin. His study in Cell biology is interdisciplinary in nature, drawing from both Cofilin and Actin remodeling.
Emil Reisler mostly deals with Actin, Biophysics, Myosin, Biochemistry and Actin-binding protein. His Actin research incorporates elements of Protein structure, Protein filament, Cofilin and Binding site. In his study, which falls under the umbrella issue of Biophysics, Enzyme is strongly linked to Polymerization.
Emil Reisler interconnects ATPase, Stereochemistry and Myofibril in the investigation of issues within Myosin. His biological study spans a wide range of topics, including Actin remodeling and Filamentous actin. His Actin remodeling study integrates concerns from other disciplines, such as Arp2/3 complex and Microfilament.
Emil Reisler mostly deals with Actin, Biophysics, Cell biology, Cofilin and Actin-binding protein. The concepts of his Actin study are interwoven with issues in Plasma protein binding, Protein filament, Actin cytoskeleton, Cytoskeleton and Protein structure. His Biophysics research is multidisciplinary, relying on both Crystallography, Biochemistry, Cysteine and Filamentous actin.
His work focuses on many connections between Cofilin and other disciplines, such as Cofilin 1, that overlap with his field of interest in Cleavage, Yeast and Subtilisin. His studies deal with areas such as ATP hydrolysis, Protomer and Actin remodeling as well as Actin-binding protein. His Actin remodeling research includes themes of Arp2/3 complex and Microfilament.
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Quantitative evaluation of the lengths of homobifunctional protein cross-linking reagents used as molecular rulers.
Nora S. Green;Emil Reisler;K.N. Houk.
Protein Science (2008)
Interpretation of equilibrium sedimentation measurements of proteins in guanidine hydrochloride solutions. Partial volumes, density increments, and the molecular weight of the subunits of rabbit muscle aldolase.
Emil Reisler;Henryk Eisenberg.
Actin filament severing by cofilin.
Dmitry Pavlov;Andras Muhlrad;John Cooper;Martin Wear.
Journal of Molecular Biology (2007)
Remodeling of actin filaments by ADF/cofilin proteins.
Vitold E. Galkin;Albina Orlova;Dmitri S. Kudryashov;Alexander Solodukhin.
Proceedings of the National Academy of Sciences of the United States of America (2011)
Cooperative role of two sulfhydryl groups in myosin adenosine triphosphatase.
Emil Reisler;Morris Burke;William F. Harrington.
Cofilin-Linked Changes in Actin Filament Flexibility Promote Severing
Brannon R McCullough;Elena E. Grintsevich;Christine K. Chen;Hyeran Kang.
Biophysical Journal (2011)
ADF/cofilin use an intrinsic mode of F-actin instability to disrupt actin filaments.
Vitold E. Galkin;Albina Orlova;Margaret S. VanLoock;Alexander Shvetsov.
Journal of Cell Biology (2003)
Dynamic properties of actin. Structural changes induced by beryllium fluoride.
A Muhlrad;P Cheung;B C Phan;C Miller.
Journal of Biological Chemistry (1994)
Bovine serum albumin in aqueous guanidine hydrochloride solutions. Preferential and absolute interactions and comparison with other systems
Emil Reisler;Yeheskiel Haik;Henryk Eisenberg.
Effect of nucleotide binding on the proximity of the essential sulfhydryl groups of myosin. Chemical probing of movement of residues during conformational transitions.
Morris Burke;Emil Reisler.
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