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Chemistry

D-Index
42
Citations
8578
World Ranking
17404
National Ranking
4264

Biology and Biochemistry

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53
Citations
9944
World Ranking
16182
National Ranking
6706

Overview

Judith S. Bond is affiliated with the University of North Carolina at Chapel Hill in the United States. Their primary research field is Biochemistry, Genetics, and Molecular Biology, with a focus on several subfields including Molecular Biology, Organic Chemistry, Public Health, Environmental and Occupational Health, Radiology, Nuclear Medicine and Imaging, as well as Literature and Literary Theory.

Their recent publications demonstrate engagement with diverse topics and notable venues. Selected publications include:

  • "A brief history of FASEB and its programs and activities" (2020, FASEB BioAdvances)
  • "To be there when the picture is being painted" (2020, Journal of Biological Chemistry)
  • "Herbert Tabor (1918-2020)*" (2020, FASEB BioAdvances)
  • "William R. Brinkley (1936-2020)" (2021, FASEB BioAdvances)
  • "Author Index" (2020, Journal of Biological Chemistry)

Judith S. Bond has frequently published in the following venues:

  • FASEB BioAdvances
  • The Journal of the Sylvia Townsend Warner Society
  • Journal of Biological Chemistry

Frequent co-authors collaborating with Bond include:

  • Greg P. Bertenshaw
  • Howard H. Garrison
  • Ralph Bradshaw
  • B.S.S. Masters

The main topics encompassed in their research cover:

  • Phytochemical Studies and Bioactivities
  • Carbohydrate Chemistry and Synthesis
  • Genetics, Bioinformatics, and Biomedical Research
  • Biotechnology and Related Fields
  • Monoclonal and Polyclonal Antibodies Research
  • Poetry Analysis and Criticism
  • Scientific Computing and Data Management

Best Publications

  • Proteases: Multifunctional Enzymes in Life and Disease

    Carlos López-Otín;Judith S. Bond

  • Proteolytic enzymes : a practical approach

    Robert J. Beynon;Judith S. Bond

  • The astacin family of metalloendopeptidases

    Judith S. Bond;Robert J. Beynon

  • Families of metalloendopeptidases and their relationships.

    Weiping Jiang;Judith S. Bond

  • Meprins, membrane-bound and secreted astacin metalloproteinases.

    Erwin E. Sterchi;Walter Stöcker;Judith S. Bond

  • The astacin family of metalloendopeptidases.

    E. Dumermuth;E. E. Sterchi;Weiping Jiang;R. L. Wolz

  • Intracellular protein catabolism

    E.A. Khairallah;J.S. Bond;J.W.C. Bird

  • Proteases: History, discovery, and roles in health and disease

    Unknown

  • Microbial-induced meprin β cleavage in MUC2 mucin and a functional CFTR channel are required to release anchored small intestinal mucus

    André Schütte;Anna Ermund;Christoph Becker-Pauly;Malin E. V. Johansson

  • Purification and characterization of a metallo-endoproteinase from mouse kidney

    R J Beynon;J D Shannon;J S Bond

  • Measuring faculty effort and contributions in medical education.

    Donald Nutter;Judith Bond;Barry Coller;Robert D'Alessandri

  • Metalloproteases meprin α and meprin β are C- and N-procollagen proteinases important for collagen assembly and tensile strength

    Claudia Broder;Philipp Arnold;Sandrine Vadon-Le Goff;Moritz A. Konerding

  • Structure of homo- and hetero-oligomeric meprin metalloproteases. Dimers, tetramers, and high molecular mass multimers.

    Greg P. Bertenshaw;Mona T. Norcum;Judith S. Bond

  • Prointerleukin-18 Is Activated by Meprin β in Vitro and in Vivo in Intestinal Inflammation

    Sanjita Banerjee;Judith S. Bond

  • Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity.

    Greg P. Bertenshaw;Benjamin E. Turk;Benjamin E. Turk;Simon J. Hubbard;Gail L. Matters

  • The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10

    Tamara Jefferson;Ulrich Auf dem Keller;Ulrich Auf dem Keller;Caroline Bellac;Verena V. Metz

  • Meprin metalloprotease expression and regulation in kidney, intestine, urinary tract infections and cancer.

    Judith S. Bond;Gail L. Matters;Sanjita Banerjee;Renee E. Dusheck

  • Metalloprotease Meprin β Generates Nontoxic N-terminal Amyloid Precursor Protein Fragments in Vivo

    Tamara Jefferson;Mirsada Čaušević;Ulrich auf dem Keller;Oliver Schilling

  • The alpha subunit of meprin A. Molecular cloning and sequencing, differential expression in inbred mouse strains, and evidence for divergent evolution of the alpha and beta subunits.

    Weiping Jiang;C. M. Gorbea;A. V. Flannery;R. J. Beynon

  • Catabolism of intracellular protein: molecular aspects.

    R. J. Beynon;J. S. Bond

  • Deletion of the Mouse Meprin β Metalloprotease Gene Diminishes the Ability of Leukocytes to Disseminate through Extracellular Matrix

    Jacqueline M. Crisman;Binzhi Zhang;Lourdes P. Norman;Judith S. Bond

Frequent Co-Authors

Robert J. Beynon
Robert J. Beynon University of Liverpool
Laurence M. Demers
Laurence M. Demers Pennsylvania State University
Simon J. Hubbard
Simon J. Hubbard Manchester Academic Health Science Centre
Christopher M. Overall
Christopher M. Overall University of British Columbia
Danny R. Welch
Danny R. Welch University of Kansas
Chella S. David
Chella S. David Mayo Clinic
Stefan Müller
Stefan Müller Otto-von-Guericke University Magdeburg
Fredrik Bäckhed
Fredrik Bäckhed University of Gothenburg
Huda Y. Zoghbi
Huda Y. Zoghbi Baylor College of Medicine

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