Research Topics
Species | P M ColmanSummaryAffiliation: The Walter and Eliza Hall Institute of Medical Research Country: Australia Publications
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Detail Information
Publications
Neuraminidase inhibitors as antiviralsP M Colman
Walter and Eliza Hall Institute of Medical Research, P O Royal Melbourne Hospital, Melbourne, VIC 3050, Australia
Vaccine 20:S55-8. 2002..Two compounds in late development (February 1999) have similar levels of potency against influenza A viruses, different routes of administration and, surprisingly, different resistance profiles both in vitro and in vivo...
Early days in drug discovery by crystallography - personal recollectionsPeter M Colman
The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia
Acta Crystallogr A 69:60-2. 2013..The 1962 Nobel Prizes for the structures of DNA and proteins marked the golden anniversary of the von Laue and Bragg discoveries...- The structural biology of type I viral membrane fusionPeter M Colman
The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3050, Australia
Nat Rev Mol Cell Biol 4:309-19. 2003..Here, we review our understanding of the structural transitions that are involved in this fusion pathway, compare it to our understanding of influenza virus membrane fusion, and discuss the implications for retroviral membrane fusion... - New antivirals and drug resistancePeter M Colman
The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia 3050
Annu Rev Biochem 78:95-118. 2009..However, other factors, such as entropy compensation and solvent anchoring, might also be exploited for improved drug design... - Zanamivir: an influenza virus neuraminidase inhibitorP M Colman
The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, 3050, Australia
Expert Rev Anti Infect Ther 3:191-9. 2005..However, patient uptake of the inhaled drug has been insufficient to conclude that drug resistance will not be an issue in the future. All zanamivir-resistant variants selected in the laboratory so far have diminished viability... 
Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitorsJ L McKimm-Breschkin
Biomolecular Research Institute, Parkville, Australia
J Virol 72:2456-62. 1998..Altered binding of the hydrophobic side chain at the 6 position or the triol group could account for the decreased binding of both the NA inhibitors and substrate...- Mutation in the influenza virus neuraminidase gene resulting in decreased sensitivity to the neuraminidase inhibitor 4-guanidino-Neu5Ac2en leads to instability of the enzymeJ L McKimm-Breschkin
Biomolecular Research Institute, Parkville, Victoria, Australia
Virology 225:240-2. 1996.... - Substrate, inhibitor, or antibody stabilizes the Glu 119 Gly mutant influenza virus neuraminidaseA Sahasrabudhe
Biomolecular Research Institute, Parkville, Victoria, Australia
Virology 247:14-21. 1998..Furthermore the presence of high levels of substrate, either cell or virus associated, may be sufficient to stabilize the NA during virus replication... - Analysis of inhibitor binding in influenza virus neuraminidaseB J Smith
Biomolecular Research Institute, Parkville, Victoria 3052, Australia
Protein Sci 10:689-96. 2001.... - Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidaseJ N Varghese
Biomolecular Research Institute 343 Royal Parade, Parkville, 3052, Australia
Structure 6:735-46. 1998..This study seeks to clarify the structural and functional consequences of replacing the glycerol sidechain of the inhibitor with other chemical constituents... - A novel approach to antiviral therapy for influenzaP M Colman
Biomolecular Research Institute, Parkville, Victoria, Australia
J Antimicrob Chemother 44:17-22. 1999..To deliver zanamivir directly to the lungs of patients the agent has been formulated for inhalation using a modified Diskhaler, which ensures high local concentrations and maximizes inhibition of viral neuraminidase... - Bax activation by Bim?P E Czabotar
The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3052, Australia
Cell Death Differ 16:1187-91. 2009..Here, we review these intriguing observations and discuss their implications for our understanding of how the BH3-only proteins initiate apoptosis... - CED-4 forms a 2 : 2 heterotetrameric complex with CED-9 until specifically displaced by EGL-1 or CED-13W D Fairlie
The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia
Cell Death Differ 13:426-34. 2006..Surprisingly, the ability of worm BH3 domains to dissociate CED-4 was specific since mammalian BH3-only proteins could not do so... - EGL-1 BH3 mutants reveal the importance of protein levels and target affinity for cell-killing potencyE F Lee
The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3050, Australia
Cell Death Differ 15:1609-18. 2008..These results demonstrate how levels of BH3-only proteins, target affinity and the spectrum of neutralization of pro-survival proteins all contribute to killing activity... - Recombinant antineuraminidase single chain antibody: expression, characterization, and crystallization in complex with antigenR L Malby
Biomolecular Research Institute, Parkville, Vic, Australia
Proteins 16:57-63. 1993..The complex between NA and the scFv has been crystallized by the vapor diffusion method. The crystals are tetragonal, space group P42(1)2, with unit cell dimensions a = b = 141 A, c = 218 A... - Virus versus antibodyP M Colman
Biomolecular Research Institute, 343 Royal Parade, Parkville, Victoria 3052, Australia
Structure 5:591-3. 1997..The fundamental characteristics of proteins and their interactions with each other suggest that this may not be so much of a constraint at all... - Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligandsM Kvansakul
The Walter and Eliza Hall Institute of Medical Research, 1G Poyal Parade, Parkville, Victoria 3050, Australia
Cell Death Differ 15:1564-71. 2008.... - The structure of the fusion glycoprotein of Newcastle disease virus suggests a novel paradigm for the molecular mechanism of membrane fusionL Chen
Biomolecular Research Institute, Parkville, Victoria 3052, Australia
Structure 9:255-66. 2001..The structure of NDV-F is fundamentally different than that of influenza virus hemagglutinin, in that the central coiled coil is in the opposite orientation with respect to the viral membrane... - The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coliT Izard
Biomolecular Research Institute, Parkville, Australia
Structure 2:361-9. 1994..The enzyme plays an important role in the regulation of sialic acid metabolism in bacteria. The reverse reaction can be exploited for the synthesis of sialic acid and some of its derivatives... - Three-dimensional structures of two plant beta-glucan endohydrolases with distinct substrate specificitiesJ N Varghese
Biomolecular Research Institute, Parkville, Victoria, Australia
Proc Natl Acad Sci U S A 91:2785-9. 1994.... - Structural studies of the resistance of influenza virus neuramindase to inhibitorsBrian J Smith
The Walter and Eliza Hall Institute of Medical Research, P O Royal Melbourne Hospital, Parkville, Victoria 3050, Australia
J Med Chem 45:2207-12. 2002..A structural explanation of the mechanism of resistance of BCX-1812, relative to zanamivir and oseltamivir in particular, is provided... - Modelling the structure of the fusion protein from human respiratory syncytial virusBrian J Smith
Biomolecular Research Institute, 343 Royal Parade, Parkville, Victoria 3052, Australia
Protein Eng 15:365-71. 2002..The location of residues involved in point mutations in several drug-resistant variants is also examined... - Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type IIIMichael C Lawrence
CSIRO Health Sciences and Nutrition, 343 Royal Parade, Parkville, VIC 3052, Australia
J Mol Biol 335:1343-57. 2004..However, in contrast to the NDV structures, we observe no ligand-induced structural changes that extend beyond the active site and modify the dimer interface... - A novel BH3 ligand that selectively targets Mcl-1 reveals that apoptosis can proceed without Mcl-1 degradationErinna F Lee
The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3050, Australia
J Cell Biol 180:341-55. 2008..Our data have important implications for the discovery of compounds that might kill cells whose survival depends on Mcl-1... - Structure of Leishmania mexicana phosphomannomutase highlights similarities with human isoformsLukasz Kedzierski
Infection and Immunity Division, The Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
J Mol Biol 363:215-27. 2006..Similarities in the structure of the parasite enzyme and its human isoforms suggest that the development of parasite-selective inhibitors will not be an easy task... - Tethered neuraminidase inhibitors that bind an influenza virus: a first step towards a diagnostic method for influenzaJennifer L McKimm-Breschkin
Biomolecular Research Institute, 343 Royal Parade, Parkville, Victoria 3052, Australia
Angew Chem Int Ed Engl 42:3118-21. 2003 - Structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparumJacqueline F Satchell
The Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia
Acta Crystallogr D Biol Crystallogr 61:1213-21. 2005.... - The trypanosomal trans-sialidase: two catalytic functions associated with one catalytic sitePeter M Colman
Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria, Australia
Structure 10:1466-8. 2002..The structure of the trypanosomal trans-sialidase reveals a canonical sialidase catalytic site elaborated with a conformational switch that creates an adjacent binding pocket for lactose...