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Chrisostomos Prodromou

Chrisostomos Prodromou

D-Index & Metrics

Biology and Biochemistry

D-Index
64
Citations
21511
World Ranking
9473
National Ranking
723

Overview

Chrisostomos Prodromou is affiliated with the University of Sussex in the United Kingdom and focuses their research within the field of Biochemistry, Genetics and Molecular Biology. Their work primarily spans molecular biology, cell biology, and materials chemistry, with additional contributions to physical and theoretical chemistry and epidemiology.

Their research topics encompass several specialized areas including heat shock proteins, endoplasmic reticulum stress and disease, enzyme structure and function, protein structure and dynamics, ATP synthase and ATPases research, thermodynamics and calorimetric analyses, as well as melanoma and MAPK pathways.

Recent publications by Chrisostomos Prodromou include several articles in notable scientific journals:

  • Chemical Perturbation of Oncogenic Protein Folding: from the Prediction of Locally Unstable Structures to the Design of Disruptors of Hsp90-Client Interactions (2020, Chemistry - A European Journal)
  • Advances towards Understanding the Mechanism of Action of the Hsp90 Complex (2022, Biomolecules)
  • The Structure-Function Relationship of Oncogenic LMTK3 (2020, Science Advances)
  • Two-Colour Single-Molecule Photoinduced Electron Transfer Fluorescence Imaging Microscopy of Chaperone Dynamics (2021, Nature Communications)
  • Structure of the TELO2-TTI1-TTI2 Complex and Its Function in TOR Recruitment to the R2TP Chaperone (2021, Cell Reports)

Chrisostomos Prodromou frequently publishes in journals including Biomolecules, Cell Stress and Chaperones, bioRxiv (Cold Spring Harbor Laboratory), Cell Reports, and Zenodo (CERN European Organization for Nuclear Research).

The scientist collaborates regularly with several coauthors, including Mehdi Mollapour, Dennis M. Bjorklund, Sarah J. Backe, Mark R. Woodford, and Dimitra Bourboulia.

Best Publications

  • Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone

    Chrisostomos Prodromou;S. Mark Roe;Ronan O'Brien;John Edward Simon Durham Ladbury

  • Structure and Mechanism of the Hsp90 Molecular Chaperone Machinery

    Laurence H. Pearl;Chrisostomos Prodromou

  • Structural Basis for Inhibition of the Hsp90 Molecular Chaperone by the Antitumor Antibiotics Radicicol and Geldanamycin

    S M Roe;C Prodromou;R O'Brien;J E Ladbury

  • Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex

    Maruf M. U. Ali;S. Mark Roe;Cara K. Vaughan;Phillipe Meyer;Phillipe Meyer

  • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

    Barry Panaretou;Chrisostomos Prodromou;S. Mark Roe;Ronan O'Brien

  • The ATPase cycle of Hsp90 drives a molecular ‘clamp’ via transient dimerization of the N-terminal domains

    Chrisostomos Prodromou;Barry Panaretou;Barry Panaretou;Shahzad Chohan;Giuliano Siligardi

  • Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1.

    Barry Panaretou;Giuliano Siligardi;Philippe Meyer;Alison Maloney

  • Structural and Functional Analysis of the Middle Segment of Hsp90 Implications for ATP Hydrolysis and Client Protein and Cochaperone Interactions

    Philippe Meyer;Chrisostomos Prodromou;Bin Hu;Cara Vaughan

  • Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones

    Chrisostomos Prodromou;Giuliano Siligardi;Ronan O'Brien;Derek N. Woolfson

  • NVP-AUY922: A Novel Heat Shock Protein 90 Inhibitor Active against Xenograft Tumor Growth, Angiogenesis, and Metastasis

    Suzanne A Eccles;Andy Massey;Florence I Raynaud;Swee Y Sharp

  • The Hsp90 molecular chaperone: an open and shut case for treatment

    Laurence H. Pearl;Chrisostomos Prodromou;Paul Workman

  • 4,5-Diarylisoxazole Hsp90 Chaperone Inhibitors: Potential Therapeutic Agents for the Treatment of Cancer

    Paul A. Brough;Wynne Aherne;Xavier Barril;Jenifer Borgognoni

  • Chaperoned Ubiquitylation-Crystal Structures of the Chip U Box E3 Ubiquitin Ligase and a Chip-Ubc13-Uev1A Complex

    Minghao Zhang;Mark Windheim;S. Mark Roe;Mark Peggie

  • Structure and in vivo function of Hsp90

    Laurence H Pearl;Chrisostomos Prodromou

  • The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)

    S.Mark Roe;Maruf M.U Ali;Philippe Meyer;Cara K Vaughan

  • Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.

    Philippe Meyer;Chrisostomos Prodromou;Chunyan Liao;Bin Hu

  • Recursive PCR: a novel technique for total gene synthesis.

    Chrisostomos Prodromou;Laurence H. Pearl

  • Structure of an Hsp90-Cdc37-Cdk4 Complex

    Cara K. Vaughan;Ulrich Gohlke;Frank Sobott;Valerie M. Good

  • Structure and functional relationships of Hsp90.

    Chrisostomos Prodromou;Laurence H Pearl

  • Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

    Giuliano Siligardi;Barry Panaretou;Philippe Meyer;Shradha Singh

Frequent Co-Authors

Laurence H. Pearl
Laurence H. Pearl University of Sussex
Peter W. Piper
Peter W. Piper University of Sheffield
S. Mark Roe
S. Mark Roe University of Sussex
Paul Workman
Paul Workman Institute of Cancer Research
Jane B. Trepel
Jane B. Trepel National Institutes of Health
Oscar Llorca
Oscar Llorca Spanish National Research Council
Leonard M. Neckers
Leonard M. Neckers National Institutes of Health
John E. Ladbury
John E. Ladbury University of Leeds
Florence I. Raynaud
Florence I. Raynaud Institute of Cancer Research
Christopher J. Moody
Christopher J. Moody University of Nottingham

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