World's Best Scientists 2026 revealed!
Andrew J. P. Docherty

Andrew J. P. Docherty

D-Index & Metrics

Biology and Biochemistry

D-Index
53
Citations
15432
World Ranking
15947
National Ranking
271

Overview

Andrew J. P. Docherty is affiliated with UCB Pharma in Belgium, where they engage in scientific research within the pharmaceutical sector. Their work is grounded in a professional environment known for the development of treatments targeting central nervous system disorders and immunology.

Though specific details on publications, co-authors, and research topics are not available, the association with UCB Pharma suggests involvement in areas related to drug discovery, clinical research, or pharmaceutical development processes. The absence of recorded publications and frequent collaborators indicates either early career development or work primarily focused on proprietary or internal research projects.

The scientist's profile does not include information on awards or book publications, suggesting their contributions have not been formally recognized through these channels or data regarding such recognitions is not accessible. Likewise, no explicit data on fields or subfields of study, as well as main topics, are listed, so the exact scientific specialization remains unspecified based on the given data.

Operating within the pharmaceutical industry in Belgium, the scientist's role may encompass laboratory research, clinical trials, or interdisciplinary collaboration, contributing to the development or optimization of pharmaceutical agents. The lack of publicly listed research outputs could reflect a focus on applied research aimed at product development rather than academic publication.

Overall, Andrew J. P. Docherty represents a contributor to pharmaceutical science operating through a major industry player, with potential involvement in specialized areas typical for UCB Pharma, including neurology and immunology-related therapeutic innovations.

Best Publications

  • Transforming growth factor beta modulates the expression of collagenase and metalloproteinase inhibitor.

    D. R. Edwards;G. Murphy;J. J. Reynolds;S. E. Whitham

  • Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity

    Andrew J. P. Docherty;Alan Lyons;Bryan J. Smith;Edwina M. Wright

  • The matrix metalloproteinases and their inhibitors.

    Gillian Murphy;Andrew J. P. Docherty

  • TNF-α converting enzyme (TACE) is inhibited by TIMP-3

    Augustin Amour;Patrick M Slocombe;Ailsa Webster;Michael Butler

  • Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP).

    G Murphy;M I Cockett;R V Ward;A J P Docherty

  • Stromelysin is an activator of procollagenase. A study with natural and recombinant enzymes.

    G Murphy;M I Cockett;P E Stephens;B J Smith

  • Comparison of human stromelysin and collagenase by cloning and sequence analysis

    S E Whitham;G Murphy;P Angel;H J Rahmsdorf

  • The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3.

    Augustin Amour;C.Graham Knight;Ailsa Webster;Patrick M. Slocombe

  • The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity.

    Gillian Murphy;Annick Houbrechts;Mark I. Cockett;Richard A. Williamson

  • The role of the C-terminal domain in collagenase and stromelysin specificity.

    G Murphy;J A Allan;F Willenbrock;M I Cockett

  • The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases

    G. Murphy;F. Willenbrock;R. V. Ward;M. I. Cockett

  • Binding of gelatinases A and B to type-I collagen and other matrix components.

    J A Allan;A J P Docherty;P J Barker;N S Huskisson

  • TISSUE INHIBITOR OF METALLOPROTEINASE-2 (TIMP-2) BINDS TO THE CATALYTIC DOMAIN OF THE CELL SURFACE RECEPTOR, MEMBRANE TYPE 1-MATRIX METALLOPROTEINASE 1 (MT1-MMP)

    Stanley Zucker;Stanley Zucker;Michelle Drews;Cathleen Conner;Hussein D. Foda;Hussein D. Foda

  • Regulation of matrix metalloproteinase activity.

    Gillian Murphy;Frances Willenbrock;Thomas Crabbe;Mark O'shea

  • Assessment of the role of the fibronectin-like domain of gelatinase A by analysis of a deletion mutant.

    G. Murphy;Quang Nguyen;M. I. Cockett;S. J. Atkinson

  • Tissue inhibitor of metalloproteinases-2 inhibits the activation of 72 kDa progelatinase by fibroblast membranes

    Robin V. Ward;Susan J. Atkinson;Patrick M. Slocombe;Andrew J.P. Docherty

  • The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A.

    Frances Willenbrock;Thomas Crabbe;Patrick M. Slocombe;Chris W. Sutton

  • Interaction of metargidin (ADAM-15) with alphavbeta3 and alpha5beta1 integrins on different haemopoietic cells.

    D. Nath;P. M. Slocombe;P. E. Stephens;A. Warn

  • The matrix metalloproteinases and their natural inhibitors: prospects for treating degenerative tissue diseases

    Andrew J.P. Docherty;James O'Connell;Tom Crabbe;Sarojani Angal

  • Meltrin gamma(ADAM-9) mediates cellular adhesion through alpha(6)beta(1 )integrin, leading to a marked induction of fibroblast cell motility.

    D. Nath;P.M. Slocombe;A. Webster;P.E. Stephens

Frequent Co-Authors

Gillian Murphy
Gillian Murphy University of Cambridge
Vera Knäuper
Vera Knäuper Cardiff University
Stanley Zucker
Stanley Zucker Stony Brook University
Vincent Everts
Vincent Everts University of Amsterdam
J J Reynolds
J J Reynolds King's College London
Carl P. Blobel
Carl P. Blobel Cornell University
John S. Mort
John S. Mort McGill University
Gideon J. Davies
Gideon J. Davies University of York
C. P. Leblond
C. P. Leblond McGill University
Robert B. Freedman
Robert B. Freedman University of Warwick

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