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Paul C. Leavis

Paul C. Leavis

Tufts University
United States

Overview

What is he best known for?

The fields of study he is best known for:

  • Amino acid
  • Biochemistry
  • Internal medicine

His primary scientific interests are in Binding site, Cell biology, Biochemistry, Troponin C and Actin. His Binding site study combines topics from a wide range of disciplines, such as Actin-binding protein, Calponin and Cooperativity. His Cell biology research integrates issues from Contractility and Actin cytoskeleton, Arp2/3 complex.

His Biochemistry research incorporates themes from Biophysics and Skeletal muscle. His studies in Troponin C integrate themes in fields like Biological activity and Plasma protein binding. His Actin research includes elements of Extracellular, Molecular biology and Kinase, MAPK/ERK pathway.

His most cited work include:

  • Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction. (361 citations)
  • Proteolytic fragments of troponin C. Localization of high and low affinity Ca2+ binding sites and interactions with troponin I and troponin T. (181 citations)
  • [10] Solute quenching of protein fluorescence (180 citations)

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

His main research concerns Biochemistry, Troponin C, Cell biology, Molecular biology and Internal medicine. His work in Biochemistry addresses subjects such as Biophysics, which are connected to disciplines such as Skeletal muscle. His work carried out in the field of Troponin C brings together such families of science as Crystallography, Troponin complex, Stereochemistry and Binding site.

The concepts of his Cell biology study are interwoven with issues in Actin-binding protein and Vascular smooth muscle. Paul C. Leavis usually deals with Molecular biology and limits it to topics linked to Kinase and Extracellular. His study on Receptor is often connected to Leptin receptor and Leukemia inhibitory factor as part of broader study in Internal medicine.

He most often published in these fields:

  • Biochemistry (41.76%)
  • Troponin C (36.26%)
  • Cell biology (37.36%)

What were the highlights of his more recent work (between 2008-2020)?

  • Cell biology (37.36%)
  • Actin (18.68%)
  • Biochemistry (41.76%)

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

His primary areas of investigation include Cell biology, Actin, Biochemistry, Tropomyosin and Actin-binding protein. Particularly relevant to Phosphorylation is his body of work in Cell biology. As part of the same scientific family, he usually focuses on Actin, concentrating on Vascular smooth muscle and intersecting with Aortic stiffness.

Paul C. Leavis works on Biochemistry which deals in particular with Protein structure. His Tropomyosin study deals with Alternative splicing intersecting with Cytoplasm, Molecular biology and Protein–protein interaction. His work in Actin-binding protein addresses issues such as Actin remodeling, which are connected to fields such as Actin remodeling of neurons, Calponin and Microfilament.

Between 2008 and 2020, his most popular works were:

  • Structure of a Longitudinal Actin Dimer Assembled by Tandem W Domains: Implications for Actin Filament Nucleation (39 citations)
  • Arginyltransferase ATE1 catalyzes midchain arginylation of proteins at side chain carboxylates in vivo. (38 citations)
  • Tropomyosin variants describe distinct functional subcellular domains in differentiated vascular smooth muscle cells. (27 citations)

In his most recent research, the most cited papers focused on:

  • Amino acid
  • Biochemistry
  • Internal medicine

Paul C. Leavis spends much of his time researching Immunoprecipitation, Scaffold protein, Smooth muscle, Phosphorylation and Cell biology. His research integrates issues of MAPK/ERK pathway and Smooth muscle tissue in his study of Immunoprecipitation.

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

Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction.

Paul C. Leavis;John Gergely;Andrew G. Szent-Gyorgyi.
CRC Critical Reviews in Biochemistry (1984)

574 Citations

Proteolytic fragments of troponin C. Localization of high and low affinity Ca2+ binding sites and interactions with troponin I and troponin T.

P C Leavis;S S Rosenfeld;J Gergely;Z Grabarek.
Journal of Biological Chemistry (1978)

289 Citations

Solute quenching of protein fluorescence.

Sherwin S. Lehrer;Paul C. Leavis.
Methods in Enzymology (1978)

262 Citations

Proteolytic fragments of troponin C. Interactions with the other troponin subunits and biological activity.

Z Grabarek;W Drabikowski;P C Leavis;S S Rosenfeld.
Journal of Biological Chemistry (1981)

197 Citations

Cooperative binding to the Ca2+-specific sites of troponin C in regulated actin and actomyosin.

Z Grabarek;J Grabarek;P C Leavis;J Gergely.
Journal of Biological Chemistry (1983)

191 Citations

Calcium-induced movement of troponin-I relative to actin in skeletal muscle thin filaments.

Terence Tao;Terence Tao;Bang-Jian Gong;Paul C. Leavis;Paul C. Leavis;Paul C. Leavis.
Science (1990)

181 Citations

Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of actin-binding proteins.

B. D. Leinweber;P. C. Leavis;P. C. Leavis;P. C. Leavis;Z. Grabarek;C.-L. A. Wang;C.-L. A. Wang.
Biochemical Journal (1999)

173 Citations

Cytoskeletal remodeling in differentiated vascular smooth muscle is actin isoform dependent and stimulus dependent

Hak Rim Kim;Cynthia Gallant;Cynthia Gallant;Paul C. Leavis;Susan J. Gunst.
American Journal of Physiology-cell Physiology (2008)

153 Citations

Effect of Ca2+ binding on troponin C. Changes in spin label mobility, extrinsic fluorescence, and sulfhydryl reactivity

J D Potter;J C Seidel;P Leavis;S S Lehrer.
Journal of Biological Chemistry (1976)

137 Citations

Metal-binding properties of calmodulin.

Chih-Lueh A. Wang;Robert R. Aquaron;Paul C. Leavis;John Gergely.
FEBS Journal (1982)

119 Citations

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