What is he best known for?
The fields of study he is best known for:
- Biochemistry
- Organic chemistry
- Ion
John Gergely mainly focuses on Myosin, Biochemistry, Biophysics, Actin and Tropomyosin.
His Myosin light-chain kinase study in the realm of Myosin connects with subjects such as Immunoglobulin light chain, Heavy chain and White.
As part of the same scientific family, John Gergely usually focuses on Biochemistry, concentrating on Troponin C and intersecting with Binding site.
He has researched Biophysics in several fields, including Staining and Anatomy.
His Actin research includes elements of Extraction and Muscle contraction.
His work deals with themes such as Rotational correlation time and Molecule, which intersect with Tropomyosin.
His most cited work include:
- Zero-length crosslinking procedure with the use of active esters (695 citations)
- Zero-length crosslinking procedure with the use of active esters (695 citations)
- Reconstitution of troponin activity from three protein components. (506 citations)
What are the main themes of his work throughout his whole career to date?
John Gergely mainly investigates Biophysics, Troponin C, Biochemistry, Actin and Myosin.
His research is interdisciplinary, bridging the disciplines of Anatomy and Biophysics.
His work carried out in the field of Troponin C brings together such families of science as Helix, Troponin complex, Conformational change, Stereochemistry and Binding site.
His work on Myofibril, Gel electrophoresis, Peptide and Adenosine triphosphate as part of general Biochemistry research is often related to White, thus linking different fields of science.
John Gergely works mostly in the field of Actin, limiting it down to topics relating to Muscle contraction and, in certain cases, Calcium, as a part of the same area of interest.
His work in the fields of Myosin, such as Myosin head and Heavy meromyosin, intersects with other areas such as Immunoglobulin light chain.
He most often published in these fields:
- Biophysics (44.90%)
- Troponin C (44.22%)
- Biochemistry (36.73%)
What were the highlights of his more recent work (between 1992-2011)?
- Actin (40.14%)
- Troponin C (44.22%)
- Biophysics (44.90%)
In recent papers he was focusing on the following fields of study:
John Gergely focuses on Actin, Troponin C, Biophysics, Troponin complex and Stereochemistry.
His Actin research incorporates elements of Crystallography and Skeletal muscle.
In his research, Inhibitory postsynaptic potential is intimately related to Biochemistry, which falls under the overarching field of Troponin C.
In the subject of general Biophysics, his work in Tropomyosin is often linked to Troponin T binding and Polyacrylamide gel electrophoresis, thereby combining diverse domains of study.
John Gergely has included themes like Antiparallel, Helix and Binding site in his Stereochemistry study.
Myosin light-chain kinase is the subject of his research, which falls under Myosin.
Between 1992 and 2011, his most popular works were:
- Photocrosslinking of benzophenone-labeled single cysteine troponin I mutants to other thin filament proteins. (46 citations)
- Residues 48 and 82 at the N-Terminal Hydrophobic Pocket of Rabbit Skeletal Muscle Troponin-C Photo-Cross-Link to Met121 of Troponin-I† (28 citations)
- Molecular Switches in Troponin (23 citations)
In his most recent research, the most cited papers focused on:
- Biochemistry
- Organic chemistry
- Ion
His scientific interests lie mostly in Actin, Troponin C, Tropomyosin, Biophysics and Stereochemistry.
His Actin study is concerned with the field of Biochemistry as a whole.
His Stereochemistry research integrates issues from Helix and Binding site.
His Myofibril study integrates concerns from other disciplines, such as Protein structure, Troponin complex and Fluorescence anisotropy.
His Actin-binding protein research is multidisciplinary, incorporating elements of MDia1, Actin remodeling and Arp2/3 complex.
His work deals with themes such as Striated muscle contraction, Myosin light-chain kinase and Molecular switch, which intersect with Nuclear magnetic resonance spectroscopy.
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