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Cross-domain inhibition of TACE ectodomain

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Standard

Cross-domain inhibition of TACE ectodomain. / Tape, Christopher J; Willems, Sofie H; Dombernowsky, Sarah L; Stanley, Peter L; Fogarasi, Marton; Ouwehand, Willem; McCafferty, John; Murphy, Gillian.

I: Proceedings of the National Academy of Sciences USA (PNAS), Bind 108, Nr. 14, 2011, s. 5578-83.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Tape, CJ, Willems, SH, Dombernowsky, SL, Stanley, PL, Fogarasi, M, Ouwehand, W, McCafferty, J & Murphy, G 2011, 'Cross-domain inhibition of TACE ectodomain', Proceedings of the National Academy of Sciences USA (PNAS), bind 108, nr. 14, s. 5578-83. https://doi.org/10.1073/pnas.1017067108

APA

Tape, C. J., Willems, S. H., Dombernowsky, S. L., Stanley, P. L., Fogarasi, M., Ouwehand, W., ... Murphy, G. (2011). Cross-domain inhibition of TACE ectodomain. Proceedings of the National Academy of Sciences USA (PNAS), 108(14), 5578-83. https://doi.org/10.1073/pnas.1017067108

Vancouver

Tape CJ, Willems SH, Dombernowsky SL, Stanley PL, Fogarasi M, Ouwehand W o.a. Cross-domain inhibition of TACE ectodomain. Proceedings of the National Academy of Sciences USA (PNAS). 2011;108(14):5578-83. https://doi.org/10.1073/pnas.1017067108

Author

Tape, Christopher J ; Willems, Sofie H ; Dombernowsky, Sarah L ; Stanley, Peter L ; Fogarasi, Marton ; Ouwehand, Willem ; McCafferty, John ; Murphy, Gillian. / Cross-domain inhibition of TACE ectodomain. I: Proceedings of the National Academy of Sciences USA (PNAS). 2011 ; Bind 108, Nr. 14. s. 5578-83.

Bibtex

@article{9f2a5654d1d5445b97476a37ed60fce8,
title = "Cross-domain inhibition of TACE ectodomain",
abstract = "Proteolytic release from the cell surface is an essential activation event for many growth factors and cytokines. TNF-a converting enzyme (TACE) is a membrane-bound metalloprotease responsible for solubilizing many pathologically significant membrane substrates and is an attractive therapeutic target for the treatment of cancer and arthritis. Prior attempts to antagonize cell-surface TACE activity have focused on small-molecule inhibition of the metalloprotease active site. Given the highly conserved nature of metalloprotease active sites, this paradigm has failed to produce a truly specific TACE inhibitor and continues to obstruct the clinical investigation of TACE activity. We report the bespoke development of a specific TACE inhibitory human antibody using {"}two-step{"} phage display. This approach combines calculated selection conditions with antibody variable-domain exchange to direct individual antibody variable domains to desired epitopes. The resulting {"}cross-domain{"} human antibody is a previously undescribed selective TACE antagonist and provides a unique alternative to small-molecule metalloprotease inhibition.",
keywords = "ADAM Proteins, Animals, Antibodies, Drug Design, Enzyme-Linked Immunosorbent Assay, Humans, Immunoglobulin Variable Region, Mice, Models, Molecular, Mutagenesis, Peptide Library, Protein Structure, Tertiary, Surface Plasmon Resonance",
author = "Tape, {Christopher J} and Willems, {Sofie H} and Dombernowsky, {Sarah L} and Stanley, {Peter L} and Marton Fogarasi and Willem Ouwehand and John McCafferty and Gillian Murphy",
year = "2011",
doi = "10.1073/pnas.1017067108",
language = "English",
volume = "108",
pages = "5578--83",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "14",

}

RIS

TY - JOUR

T1 - Cross-domain inhibition of TACE ectodomain

AU - Tape, Christopher J

AU - Willems, Sofie H

AU - Dombernowsky, Sarah L

AU - Stanley, Peter L

AU - Fogarasi, Marton

AU - Ouwehand, Willem

AU - McCafferty, John

AU - Murphy, Gillian

PY - 2011

Y1 - 2011

N2 - Proteolytic release from the cell surface is an essential activation event for many growth factors and cytokines. TNF-a converting enzyme (TACE) is a membrane-bound metalloprotease responsible for solubilizing many pathologically significant membrane substrates and is an attractive therapeutic target for the treatment of cancer and arthritis. Prior attempts to antagonize cell-surface TACE activity have focused on small-molecule inhibition of the metalloprotease active site. Given the highly conserved nature of metalloprotease active sites, this paradigm has failed to produce a truly specific TACE inhibitor and continues to obstruct the clinical investigation of TACE activity. We report the bespoke development of a specific TACE inhibitory human antibody using "two-step" phage display. This approach combines calculated selection conditions with antibody variable-domain exchange to direct individual antibody variable domains to desired epitopes. The resulting "cross-domain" human antibody is a previously undescribed selective TACE antagonist and provides a unique alternative to small-molecule metalloprotease inhibition.

AB - Proteolytic release from the cell surface is an essential activation event for many growth factors and cytokines. TNF-a converting enzyme (TACE) is a membrane-bound metalloprotease responsible for solubilizing many pathologically significant membrane substrates and is an attractive therapeutic target for the treatment of cancer and arthritis. Prior attempts to antagonize cell-surface TACE activity have focused on small-molecule inhibition of the metalloprotease active site. Given the highly conserved nature of metalloprotease active sites, this paradigm has failed to produce a truly specific TACE inhibitor and continues to obstruct the clinical investigation of TACE activity. We report the bespoke development of a specific TACE inhibitory human antibody using "two-step" phage display. This approach combines calculated selection conditions with antibody variable-domain exchange to direct individual antibody variable domains to desired epitopes. The resulting "cross-domain" human antibody is a previously undescribed selective TACE antagonist and provides a unique alternative to small-molecule metalloprotease inhibition.

KW - ADAM Proteins

KW - Animals

KW - Antibodies

KW - Drug Design

KW - Enzyme-Linked Immunosorbent Assay

KW - Humans

KW - Immunoglobulin Variable Region

KW - Mice

KW - Models, Molecular

KW - Mutagenesis

KW - Peptide Library

KW - Protein Structure, Tertiary

KW - Surface Plasmon Resonance

U2 - 10.1073/pnas.1017067108

DO - 10.1073/pnas.1017067108

M3 - Journal article

C2 - 21415364

VL - 108

SP - 5578

EP - 5583

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 14

ER -

ID: 38029041