World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
50
Citations
11003
World Ranking
17522
National Ranking
7195

Overview

Fred Dyda is affiliated with the National Institutes of Health in the United States and has contributed to research primarily in the field of Biochemistry, Genetics and Molecular Biology. Their work spans several subfields, with a substantial focus on Molecular Biology, followed by Plant Science, Genetics, Ecology, and Molecular Medicine.

Their research topics include:

  • CRISPR and Genetic Engineering
  • Advanced biosensing and bioanalysis techniques
  • Chromosomal and Genetic Variations
  • Bacterial Genetics and Biotechnology
  • Biochemical and Molecular Research
  • RNA Interference and Gene Delivery
  • Bacteriophages and microbial interactions

Dyda's recent published papers illustrate contributions across multiple areas of molecular biology and genetics. Notable papers include:

  • "Structural basis of seamless excision and specific targeting by piggyBac transposase" (2020), published in Nature Communications
  • "Comment on 'RNA-guided DNA insertion with CRISPR-associated transposases'" (2020), published in Science
  • "Structural Basis for a Dual Function ATP Grasp Ligase That Installs Single and Bicyclic ω-Ester Macrocycles in a New Multicore RiPP Natural Product" (2021), published in Journal of the American Chemical Society
  • "Structures of IS C th4 transpososomes reveal the role of asymmetry in copy-out/paste-in DNA transposition" (2020), published in The EMBO Journal
  • "The large bat Helitron DNA transposase forms a compact monomeric assembly that buries and protects its covalently bound 5'-transposon end" (2021), published in Molecular Cell

Frequent publication venues where Dyda has appeared include:

  • Faculty Opinions - Post-Publication Peer Review of the Biomedical Literature
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Nature Communications
  • Nucleic Acids Research
  • Journal of Biological Chemistry

Collaboration has been an essential aspect of their research. Frequent co-authors working alongside Dyda include:

  • Alison B. Hickman
  • Dalibor Košek
  • Christopher M. Furman
  • Wentian Luo
  • Matthew H. Wilson

Best Publications

  • Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases.

    Fred Dyda;Alison B. Hickman;Timothy M. Jenkins;Alan Engelman

  • Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer's β-Amyloid Peptide, and Structural Characterization by Solid State NMR†

    John J. Balbach;Yoshitaka Ishii;Oleg N. Antzutkin;Richard D. Leapman

  • GCN5-RELATED N-ACETYLTRANSFERASES: A Structural Overview

    Fred Dyda;David C. Klein;Alison Burgess Hickman

  • Three new structures of the core domain of HIV-1 integrase: an active site that binds magnesium.

    Yehuda Goldgur;Fred Dyda;Alison B. Hickman;Timothy M. Jenkins

  • Crystal Structure of the 14-3-3ζ:Serotonin N-Acetyltransferase Complex: A Role for Scaffolding in Enzyme Regulation

    Tomas Obsil;Rodolfo Ghirlando;David C Klein;Surajit Ganguly

  • Solid State NMR Reveals a pH-dependent Antiparallel β-Sheet Registry in Fibrils Formed by a β-Amyloid Peptide

    A.T. Petkova;G. Buntkowsky;F. Dyda;R.D. Leapman

  • G domain dimerization controls dynamin's assembly-stimulated GTPase activity

    Joshua S. Chappie;Sharmistha Acharya;Marilyn Leonard;Sandra L. Schmid

  • Breaking and joining single-stranded DNA: the HUH endonuclease superfamily.

    Michael Chandler;Fernando de la Cruz;Fred Dyda;Alison B. Hickman

  • Insertion Sequence IS26 Reorganizes Plasmids in Clinically Isolated Multidrug-Resistant Bacteria by Replicative Transposition

    Susu He;Alison Burgess Hickman;Alessandro M. Varani;Patricia Siguier

  • A pseudoatomic model of the dynamin polymer identifies a hydrolysis-dependent powerstroke.

    Joshua S. Chappie;Jason A. Mears;Jason A. Mears;Shunming Fang;Marilyn Leonard

  • Catalytic domain of human immunodeficiency virus type 1 integrase: identification of a soluble mutant by systematic replacement of hydrophobic residues.

    Timothy M. Jenkins;Alison B. Hickman;Fred Dyda;Rodolfo Ghirlando

  • The Structural Basis of Ordered Substrate Binding by Serotonin N-Acetyltransferase: Enzyme Complex at 1.8 Å Resolution with a Bisubstrate Analog

    Alison Burgess Hickman;M.A.A. Namboodiri;M.A.A. Namboodiri;David C. Klein;Fred Dyda

  • Molecular Organization in Site-Specific Recombination: The Catalytic Domain of Bacteriophage HP1 Integrase at 2.7 Å Resolution

    Alison Burgess Hickman;Shani Waninger;John J Scocca;Fred Dyda

  • Structural unity among viral origin binding proteins: crystal structure of the nuclease domain of adeno-associated virus Rep.

    Alison Burgess Hickman;Donald R Ronning;Robert M Kotin;Fred Dyda

  • A Model for Transposition of the Colistin Resistance Gene mcr-1 by ISApl1

    Erik Snesrud;Susu He;Michael Chandler;John P. Dekker

  • Molecular architecture of a eukaryotic DNA transposase

    Alison B Hickman;Zhanita N Perez;Liqin Zhou;Primrose Musingarimi;Primrose Musingarimi

  • Integrating prokaryotes and eukaryotes: DNA transposases in light of structure

    Alison Burgess Hickman;Michael Chandler;Fred Dyda

  • Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register β-sheet structure

    Reed B. Wickner;Fred Dyda;Robert Tycko

  • Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism.

    Alison Burgess Hickman;David C. Klein;Fred Dyda

  • Transposition of hAT elements links transposable elements and V(D)J

    Rupak Mitra;Peter W. Atkinson;Alison Burgess Hickman;Fred Dyda

Frequent Co-Authors

David C. Klein
David C. Klein National Institutes of Health
Michael Chandler
Michael Chandler Georgetown University Medical Center
Nancy L. Craig
Nancy L. Craig Johns Hopkins University School of Medicine
Rodolfo Ghirlando
Rodolfo Ghirlando National Institutes of Health
David R. Davies
David R. Davies National Institutes of Health
Robert Craigie
Robert Craigie National Institutes of Health
Robert Tycko
Robert Tycko National Institutes of Health
Sandra L. Schmid
Sandra L. Schmid The University of Texas Southwestern Medical Center
Ronald A. Milligan
Ronald A. Milligan Scripps Research Institute
Reed B. Wickner
Reed B. Wickner National Institutes of Health

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