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
Biology and Biochemistry D-index 49 Citations 10,942 86 World Ranking 13521 National Ranking 5719

Overview

What is he best known for?

The fields of study he is best known for:

  • Gene
  • Enzyme
  • Amino acid

Wayne A. Fenton focuses on Biochemistry, GroEL, Chaperonin, Protein folding and GroES. His study looks at the relationship between Biochemistry and fields such as Biophysics, as well as how they intersect with chemical problems. His Protein folding study combines topics in areas such as Thermosome and Foldase.

His research in Foldase focuses on subjects like GroES Protein, which are connected to GroEL Protein, Operon and Protein biosynthesis. He merges GroES with Opposite ring in his study. His studies in ATP hydrolysis integrate themes in fields like Folding and Binding site.

His most cited work include:

  • Residues in chaperonin GroEL required for polypeptide binding and release (572 citations)
  • STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING (503 citations)
  • Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes (379 citations)

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

His primary scientific interests are in Biochemistry, GroEL, Chaperonin, GroES and Biophysics. His Biochemistry study frequently links to related topics such as Molecular biology. His GroEL research is multidisciplinary, incorporating perspectives in Crystallography, Folding and Cryo-electron microscopy.

His Chaperonin study is focused on Protein folding in general. His GroES research integrates issues from RuBisCO, Cooperativity, Adenosine triphosphate and Nucleotide. The various areas that he examines in his Biophysics study include ATP hydrolysis, ATPase, Plasma protein binding, Chaperone and Allosteric regulation.

He most often published in these fields:

  • Biochemistry (59.55%)
  • GroEL (41.57%)
  • Chaperonin (35.96%)

What were the highlights of his more recent work (between 2004-2020)?

  • GroEL (41.57%)
  • Biophysics (38.20%)
  • Chaperonin (35.96%)

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

The scientist’s investigation covers issues in GroEL, Biophysics, Chaperonin, GroES and Biochemistry. His GroEL research incorporates themes from Folding, Molecular physics, Crystallography and Cryo-electron microscopy. His work deals with themes such as ATP hydrolysis, ATPase, Protein subunit, Chaperone and Allosteric regulation, which intersect with Biophysics.

His Chaperonin study contributes to a more complete understanding of Protein folding. His GroES research incorporates elements of Nucleotide and RuBisCO. The concepts of his Biochemistry study are interwoven with issues in Motor neuron and Cell biology.

Between 2004 and 2020, his most popular works were:

  • Two Families of Chaperonin: Physiology and Mechanism (346 citations)
  • Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. (210 citations)
  • Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. (210 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

Residues in chaperonin GroEL required for polypeptide binding and release

Fenton Wa;Kashi Y;Furtak K;Horwich Al.
Nature (1994)

771 Citations

STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING

Paul B. Sigler;Zhaohui Xu;Hays S. Rye;Steven G. Burston.
Annual Review of Biochemistry (1998)

686 Citations

Two Families of Chaperonin: Physiology and Mechanism

Arthur L. Horwich;Wayne A. Fenton;Eli Chapman;George W. Farr.
Annual Review of Cell and Developmental Biology (2007)

503 Citations

Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

Jonathan S. Weissman;Jonathan S. Weissman;Corinne M. Hohl;Corinne M. Hohl;Oleg Kovalenko;Yechezkel Kashi.
Cell (1995)

499 Citations

GroEL-mediated protein folding.

Wayne A. Fenton;Arthur L. Horwich.
Protein Science (1997)

488 Citations

Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL

Arthur L. Horwich;K.Brooks Low;Wayne A. Fenton;Irvin N. Hirshfield.
Cell (1993)

470 Citations

Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction

Jonathan S Weissman;Jonathan S Weissman;Hays S Rye;Hays S Rye;Wayne A Fenton;Joseph M Beechem.
Cell (1996)

453 Citations

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

Jonathan S. Weissman;Yechezkel Kashi;Wayne A. Fenton;Arthur L. Horwich.
Cell (1994)

418 Citations

GroEL-GroES Cycling: ATP and Nonnative Polypeptide Direct Alternation of Folding-Active Rings

Hays S. Rye;Hays S. Rye;Alan M. Roseman;Shaoxia Chen;Krystyna Furtak;Krystyna Furtak.
Cell (1999)

368 Citations

Structure and expression of a complementary DNA for the nuclear coded precursor of human mitochondrial ornithine transcarbamylase.

Arthur L. Horwich;Wayne A. Fenton;Kenneth R. Williams;Frantisek Kalousek.
Science (1984)

337 Citations

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