James C. Whisstock

ORCID: 0000-0003-4200-5611
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About
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Research Areas
  • Protease and Inhibitor Mechanisms
  • Blood Coagulation and Thrombosis Mechanisms
  • Peptidase Inhibition and Analysis
  • Enzyme Structure and Function
  • Signaling Pathways in Disease
  • Calpain Protease Function and Regulation
  • Glycosylation and Glycoproteins Research
  • Monoclonal and Polyclonal Antibodies Research
  • Machine Learning in Bioinformatics
  • Protein Structure and Dynamics
  • Autoimmune and Inflammatory Disorders Research
  • Enzyme Production and Characterization
  • RNA and protein synthesis mechanisms
  • Cellular transport and secretion
  • Genomics and Phylogenetic Studies
  • Complement system in diseases
  • Streptococcal Infections and Treatments
  • Advanced Electron Microscopy Techniques and Applications
  • Coagulation, Bradykinin, Polyphosphates, and Angioedema
  • Toxin Mechanisms and Immunotoxins
  • Venomous Animal Envenomation and Studies
  • Endoplasmic Reticulum Stress and Disease
  • Biochemical and Structural Characterization
  • Acute Lymphoblastic Leukemia research
  • Invertebrate Immune Response Mechanisms

Monash University
2015-2024

Australian Regenerative Medicine Institute
2015-2024

Australian National University
2020-2024

ARC Centre of Excellence in Advanced Molecular Imaging
2014-2023

EMBL Australia
2019-2023

New York Structural Biology Center
2023

Australian Research Council
2013-2022

Australian Cancer Research Foundation
2021-2022

Discovery Institute
2019-2021

Southeast University
2019-2020

Abstract Multiple structural alignment is a fundamental problem in genomics. In this article, we define reliable and robust algorithm, MUSTANG (MUltiple STructural AligNment AlGorithm), for the of multiple protein structures. Given set structures, program constructs using spatial information C α atoms set. Broadly based on progressive pairwise heuristic, algorithm gains accuracy through novel effective refinement phases. reports sequence corresponding superposition Alignments generated by...

10.1002/prot.20921 article EN Proteins Structure Function and Bioinformatics 2006-05-30

James A. Irving1, Robert N. Pike1, Arthur M. Lesk2, and C. Whisstock1,3 1Department of Biochemistry Molecular Biology, Monash University, Clayton Campus, Melbourne, Victoria 3168, Australia; 2Wellcome Trust Centre for the Study Mechanisms in Disease, Cambridge Institute Medical Research, University Clinical School, CB2 2XY, United Kingdom

10.1101/gr.gr-1478r article EN cc-by-nc Genome Research 2000-11-21

The ability to catalytically cleave protein substrates after synthesis is fundamental for all forms of life. Accordingly, site-specific proteolysis one the most important post-translational modifications. key understanding physiological role a protease identify its natural substrate(s). Knowledge substrate specificity can dramatically improve our predict target substrates, but this information must be utilized in an effective manner order efficiently by silico approaches. To address problem,...

10.1371/journal.pone.0050300 article EN cc-by PLoS ONE 2012-11-29

Glycosylation is a ubiquitous type of protein post-translational modification (PTM) in eukaryotic cells, which plays vital roles various biological processes (BPs) such as cellular communication, ligand recognition and subcellular recognition. It estimated that >50% the entire human proteome glycosylated. However, it still significant challenge to identify glycosylation sites, requires expensive/laborious experimental research. Thus, bioinformatics approaches can predict glycan occupancy at...

10.1093/bioinformatics/btu852 article EN Bioinformatics 2015-01-06

Proteins containing membrane attack complex/perforin (MACPF) domains play important roles in vertebrate immunity, embryonic development, and neural-cell migration. In vertebrates, the ninth component of complement perforin form oligomeric pores that lyse bacteria kill virus-infected cells, respectively. However, mechanism MACPF function is unknown. We determined crystal structure a bacterial protein, Plu-MACPF from Photorhabdus luminescens , to 2.0 angstrom resolution. The domain reveals...

10.1126/science.1144706 article EN Science 2007-08-24

Many bacterial pathogens utilize a type III secretion system to deliver multiple effector proteins into host cells. Here we found that the effectors, NleE from enteropathogenic E. coli (EPEC) and OspZ Shigella, blocked translocation of p65 subunit transcription factor, NF-κB, cell nucleus. NF-κB inhibition by was associated with decreased IL-8 expression in EPEC-infected intestinal epithelial Ectopically expressed also nuclear c-Rel, but not p50 or STAT1/2. homologues other attaching...

10.1371/journal.ppat.1000898 article EN cc-by PLoS Pathogens 2010-05-13

Plasminogen is the proenzyme precursor of primary fibrinolytic protease plasmin. Circulating plasminogen, which comprises a Pan-apple (PAp) domain, five kringle domains (KR1-5), and serine (SP) adopts closed, activation-resistant conformation. The mediate interactions with fibrin clots cell-surface receptors. These trigger plasminogen to adopt an open form that can be cleaved converted plasmin by tissue-type urokinase-type activators. Here, structure closed reveals PAp SP domains, together...

10.1016/j.celrep.2012.02.012 article EN cc-by Cell Reports 2012-03-01

Expansion of "low complex" repeats amino acids such as glutamine (Poly-Q) is associated with protein misfolding and the development degenerative diseases Huntington's disease. The mechanism by which regions promote remains controversial, function many repeat-containing proteins (RCPs) obscure, role (if any) repeat to be determined. Here, a Web-accessible database RCPs presented. distribution evolution that contain homopeptide tracts are considered, existence functional patterns investigated....

10.1101/gr.3096505 article EN cc-by-nc Genome Research 2005-04-01
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