G. Chelvanayagam

发表

Easy adaptation of protein structure to sequence.

G. Chelvanayagam, G. Roy, P. Argos, 1994, Protein engineering.

Anatomy and evolution of proteins displaying the viral capsid jellyroll topology.

G. Chelvanayagam, P. Argos, J. Heringa, 1992, Journal of molecular biology.

An analysis of simultaneous variation in protein structures.

G. Chelvanayagam, G. Gonnet, S. Benner, 1997, Protein engineering.

A roadmap for HLA-A, HLA-B, and HLA-C peptide binding specificities

G. Chelvanayagam, 1996, Immunogenetics.

A roadmap for HLA-DR peptide binding specificities.

G Chelvanayagam, G. Chelvanayagam, 1997, Human immunology.

Peptide binding motifs and specificities for HLA-DQ molecules

G. Chelvanayagam, G. Chelvanayagam, Xiao-jiang Gao, 1999, Immunogenetics.

Identification, Characterization, and Crystal Structure of the Omega Class Glutathione Transferases*

G Chelvanayagam, G. Chelvanayagam, D. Danley, 2000, The Journal of Biological Chemistry.

An analysis of the helix‐to‐strand transition between peptides with identical sequence

G Chelvanayagam, G Folkers, G. Chelvanayagam, 2000, Proteins.

Ab initio calculations on hidden modulators of theta class glutathione transferase activity

G. Chelvanayagam, M. Parker, J. Flanagan, 2000, Proteins.

Mutagenic analysis of conserved arginine residues in and around the novel sulfate binding pocket of the human Theta class glutathione transferase T2‐2

G. Chelvanayagam, J. Rossjohn, M. Parker, 1999, Protein science : a publication of the Protein Society.

Peptides: two-faced, cheating go-betweens? Limits in the cellular immune system

G. Chelvanayagam, S. Easteal, 1997, Immunogenetics.

HLA class I alleles in Australian aborigines and their peptide binding profiles

G. Chelvanayagam, J. McCluskey, Xiao-jiang Gao, 2000 .

Structural comparison of major histocompatibility complex class I molecules and homology modelling of five distinct human leukocyte antigen-A alleles.

G. Chelvanayagam, S. Easteal, X. Gao, 1996, Protein engineering.

Polymorphism of phase II enzymes: identification of new enzymes and polymorphic variants by database analysis.

G. Chelvanayagam, L. Jermiin, A. Blackburn, 1998, Toxicology letters.

Proteolytic processing of peptides in the lumen of the endoplasmic reticulum for antigen presentation by major histocompatibility class I

G. Chelvanayagam, A. Müllbacher, M. Lobigs, 2000, European journal of immunology.

Fly fishing for GSTs: a unified nomenclature for mammalian and insect glutathione transferases

G. Chelvanayagam, M. Parker, P. Board, 2001 .

Correlating sequence variation with HLA‐A allelic families: Implications for T cell receptor binding specificities

G. Chelvanayagam, S. Easteal, X. Gao, 1998, Immunology and cell biology.

Peptide mimics of a tumor antigen induce functional cytotoxic T cells

G. Chelvanayagam, V. Apostolopoulos, M. Sandrin, 1998, Nature Biotechnology.

The Peopling of New Guinea: Evidence from Class I Human Leukocyte Antigen

G. Chelvanayagam, X. Gao, R. Attenborough, 2001, Human biology.

Subunit: Its Effects on Protein Structure and Function A Novel Asn344 Deletion in the Core Domain of Coagulation Factor XIII A

G. Chelvanayagam, R. Baker, P. Yenchitsomanus, 2013 .

Identification and characterization of two missense mutations causing factor XIIIA deficiency

G. Chelvanayagam, R. Baker, P. Kuperan, 1999, British journal of haematology.

A novel Asn344 deletion in the core domain of coagulation factor XIII A subunit: its effects on protein structure and function.

G. Chelvanayagam, R. Baker, P. Yenchitsomanus, 1998, Blood.

A Novel Asn 344 Deletion in the Core Domain of Coagulation Factor XIII A Subunit : Its Effects on Protein Structure and Function

G. Chelvanayagam, R. Baker, P. Yenchitsomanus, 1998 .

Deletion in the Core Domain of Coagulation Factor XIII A Subunit : Its Effects on Protein Structure and Function

G. Chelvanayagam, R. Baker, P. Yenchitsomanus, 1998 .

MUC1 Peptides Presented by Class I H2 and Anti-MUC1 Antibodies React Directly with

G. Chelvanayagam, V. Apostolopoulos, I. Mckenzie, 2017 .

Anti-MUC1 antibodies react directly with MUC1 peptides presented by class I H2 and HLA molecules.

G. Chelvanayagam, V. Apostolopoulos, I. Mckenzie, 1998, Journal of immunology.

MUC 1 Peptides Presented by Class I H 2 and Anti-MUC 1 Antibodies React Directly with and

G. Chelvanayagam, V. Apostolopoulos, I. Mckenzie, 1998 .

Human Glutathione Transferase T2-2 Discloses Some Evolutionary Strategies for Optimization of the Catalytic Activity of Glutathione Transferases*

G. Chelvanayagam, R. Paolesse, M. Parker, 2001, The Journal of Biological Chemistry.

Identification of novel glutathione transferases and polymorphic variants by expressed sequence tag database analysis.

G. Chelvanayagam, L. Jermiin, A. Blackburn, 2001, Drug metabolism and disposition: the biological fate of chemicals.

Database Analysis and Gene Discovery in Pharmacogenetics

G. Chelvanayagam, A. Blackburn, N. Tetlow, 2000, Clinical chemistry and laboratory medicine.

The Glutathione Transferase Structural Family Includes a Nuclear Chloride Channel and a Ryanodine Receptor Calcium Release Channel Modulator*

G. Chelvanayagam, P. Gage, A. Dulhunty, 2001, The Journal of Biological Chemistry.

The Ubp6 family of deubiquitinating enzymes contains a ubiquitin‐like domain: SUb

G. Chelvanayagam, R. Baker, A. Wyndham, 1999, Protein science : a publication of the Protein Society.

Correlating patterns in alignments of polymorphic sequences with experimental assays

Simon Easteal, G. Chelvanayagam, G. Chelvanayagam, 1997, Comput. Appl. Biosci..

Zeta, a novel class of glutathione transferases in a range of species from plants to humans.

G. Chelvanayagam, L. Jermiin, R. Baker, 1997, The Biochemical journal.

Bona Fide Predictions of Protein Secondary Structure Using Transparent Analyses of Multiple Sequence Alignments.

Marcel Turcotte, Steven A. Benner, Gina Cannarozzi, 1997, Chemical reviews.

Structural characteristics and stabilizing principles of bent β‐strands in protein tertiary architectures

G. Chelvanayagam, P. Argos, Carola Daffner, 1994, Protein science : a publication of the Protein Society.

Bona Fide Predictions of Protein Secondary Structure Using Transparent Analyses of Multiple Sequence Alignments

Marcel Turcotte, Dietlind L. Gerloff, Steven A. Benner, 1998 .

A viral peptide with limited homology to a self peptide can induce clinical signs of experimental autoimmune encephalomyelitis.

G. Chelvanayagam, L. Steinman, R. Liblau, 1998, Journal of immunology.

A combinatorial distance-constraint approach to predicting protein tertiary models from known secondary structure.

G Chelvanayagam, L Knecht, T Jenny, 1998, Folding & design.

Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site.

G Chelvanayagam, J Rossjohn, M W Parker, 1998, Structure.

Dichloromethane mediated in vivo selection and functional characterization of rat glutathione S-transferase theta 1-1 variants.

G. Chelvanayagam, S. Vuilleumier, J. Rossjohn, 2001, European journal of biochemistry.

Prediction of protein folding pathways: Bovine pancreatic trypsin inhibitor

G. Chelvanayagam, P. Argos, 2004, Cytotechnology.

Homology models for the PERB11 multigene family.

G. Chelvanayagam, J. Lalonde, A. Monaco, 1998, Folding & design.

Prediction of protein folding pathways.

G. Chelvanayagam, P. Argos, R. Bringas, 1992, Journal of molecular biology.

Homology model for the human GSTT2 theta class glutathione transferase

G. Chelvanayagam, M. Parker, M. Wilce, 1997, Proteins.

The phospho‐β‐galactosidase and synaptotagmin predictions

Dietlind L. Gerloff, Steven A. Benner, G. Chelvanayagam, 1995 .

Identification of a new mutation (Gly420Ser), distal to the active site, that leads to factor XIII deficiency

G. Chelvanayagam, P. Yenchitsomanus, P. Board, 2000, European journal of haematology.

A homology model for the human theta‐class glutathione transferase T1–1

G Chelvanayagam, J Rossjohn, M W Parker, 1998, Proteins.

Mutagenesis of the active site of the human Theta-class glutathione transferase GSTT2-2: catalysis with different substrates involves different residues.

G Chelvanayagam, M W Parker, G. Chelvanayagam, 1996, The Biochemical journal.