D-Index & Metrics Best Publications

D-Index & Metrics D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines.

Discipline name D-index D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines. Citations Publications World Ranking National Ranking
Chemistry D-index 51 Citations 6,845 179 World Ranking 10422 National Ranking 2949
Biology and Biochemistry D-index 54 Citations 7,858 196 World Ranking 11262 National Ranking 4854

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Biochemistry
  • Amino acid

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.

His most cited work include:

  • Quantitative evaluation of the lengths of homobifunctional protein cross-linking reagents used as molecular rulers. (206 citations)
  • Remodeling of actin filaments by ADF/cofilin proteins. (160 citations)
  • 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. (159 citations)

What are the main themes of his work throughout his whole career to date?

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.

He most often published in these fields:

  • Actin (69.35%)
  • Biophysics (44.72%)
  • Myosin (40.20%)

What were the highlights of his more recent work (between 2009-2021)?

  • Actin (69.35%)
  • Biophysics (44.72%)
  • Cell biology (18.59%)

In recent papers he was focusing on the following fields of study:

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.

Between 2009 and 2021, his most popular works were:

  • Remodeling of actin filaments by ADF/cofilin proteins. (160 citations)
  • Cofilin-Linked Changes in Actin Filament Flexibility Promote Severing (110 citations)
  • Atomic force microscopy reveals drebrin induced remodeling of f-actin with subnanometer resolution. (74 citations)

This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.

Best Publications

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)

322 Citations

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.
Biochemistry (1969)

247 Citations

Actin filament severing by cofilin.

Dmitry Pavlov;Andras Muhlrad;John Cooper;Martin Wear.
Journal of Molecular Biology (2007)

209 Citations

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)

196 Citations

Cooperative role of two sulfhydryl groups in myosin adenosine triphosphatase.

Emil Reisler;Morris Burke;William F. Harrington.
Biochemistry (1974)

164 Citations

Cofilin-Linked Changes in Actin Filament Flexibility Promote Severing

Brannon R McCullough;Elena E. Grintsevich;Christine K. Chen;Hyeran Kang.
Biophysical Journal (2011)

153 Citations

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)

147 Citations

Dynamic properties of actin. Structural changes induced by beryllium fluoride.

A Muhlrad;P Cheung;B C Phan;C Miller.
Journal of Biological Chemistry (1994)

143 Citations

Bovine serum albumin in aqueous guanidine hydrochloride solutions. Preferential and absolute interactions and comparison with other systems

Emil Reisler;Yeheskiel Haik;Henryk Eisenberg.
Biochemistry (1977)

133 Citations

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.
Biochemistry (1977)

132 Citations

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