Michael W. Parker
Michael W. Parker
St Vincent's Institute of Medical Research and The University of Melbourne
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Cited by
Cited by
Structure and function of glutathione S-transferases
MCJ Wilce, MW Parker
Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular…, 1994
Pore-forming protein toxins: from structure to function
MW Parker, SC Feil
Progress in biophysics and molecular biology 88 (1), 91-142, 2005
Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
J Rossjohn, SC Feil, WJ McKinstry, RK Tweten, MW Parker
Cell 89 (5), 685-692, 1997
AMPK β subunit targets metabolic stress sensing to glycogen
G Polekhina, A Gupta, BJ Michell, B Van Denderen, S Murthy, SC Feil, ...
Current biology 13 (10), 867-871, 2003
Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states
MW Parker, JT Buckley, JPM Postma, AD Tucker, K Leonard, F Pattus, ...
Nature 367 (6460), 292-295, 1994
Model for growth hormone receptor activation based on subunit rotation within a receptor dimer
RJ Brown, JJ Adams, RA Pelekanos, Y Wan, WJ McKinstry, K Palethorpe, ...
Nature structural & molecular biology 12 (9), 814-821, 2005
Mechanism of activation of protein kinase JAK2 by the growth hormone receptor
AJ Brooks, W Dai, ML O’Mara, D Abankwa, Y Chhabra, RA Pelekanos, ...
Science 344 (6185), 1249783, 2014
The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins
O Shatursky, AP Heuck, LA Shepard, J Rossjohn, MW Parker, ...
Cell 99 (3), 293-299, 1999
Structure of the membrane-pore-forming fragment of colicin A
MW Parker, F Pattus, AD Tucker, D Tsernoglou
Nature 337 (6202), 93-96, 1989
Structure of the Alzheimer's disease amyloid precursor protein copper binding domain: a regulator of neuronal copper homeostasis
KJ Barnham, WJ McKinstry, G Multhaup, D Galatis, CJ Morton, CC Curtain, ...
Journal of Biological Chemistry 278 (19), 17401-17407, 2003
Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: an α-helical to β-sheet transition identified…
LA Shepard, AP Heuck, BD Hamman, J Rossjohn, MW Parker, KR Ryan, ...
Biochemistry 37 (41), 14563-14574, 1998
The structure of the GM-CSF receptor complex reveals a distinct mode of cytokine receptor activation
G Hansen, TR Hercus, BJ McClure, FC Stomski, M Dottore, J Powell, ...
Cell 134 (3), 496-507, 2008
Three-dimensional structure of class π glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 resolution
P Reinemer, HW Dirr, R Ladenstein, R Huber, ML Bello, G Federici, ...
Journal of molecular biology 227 (1), 214-226, 1992
The granulocyte-macrophage colony-stimulating factor receptor: linking its structure to cell signaling and its role in disease
TR Hercus, D Thomas, MA Guthridge, PG Ekert, J King-Scott, MW Parker, ...
Blood, The Journal of the American Society of Hematology 114 (7), 1289-1298, 2009
Oncogenic protein interfaces: small molecules, big challenges
TL Nero, CJ Morton, JK Holien, J Wielens, MW Parker
Nature Reviews Cancer 14 (4), 248-262, 2014
Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein
J Rossjohn, R Cappai, SC Feil, A Henry, WJ McKinstry, D Galatis, ...
Nature structural biology 6 (4), 327-331, 1999
A Systematic and Functional Classification of Streptococcus pyogenes That Serves as a New Tool for Molecular Typing and Vaccine Development
M Sanderson-Smith, DMP De Oliveira, J Guglielmini, DJ McMillan, T Vu, ...
The Journal of infectious diseases 210 (8), 1325-1338, 2014
Crystal structure of a theta‐class glutathione transferase.
MC Wilce, PG Board, SC Feil, MW Parker
The EMBO journal 14 (10), 2133-2143, 1995
Zanamivir-resistant influenza viruses with a novel neuraminidase mutation
AC Hurt, JK Holien, M Parker, A Kelso, IG Barr
Journal of virology 83 (20), 10366-10373, 2009
Iron‐and manganese‐containing superoxide dismutases can be distinguished by analysis of their primary structures
MW Parker, CCF Blake
FEBS letters 229 (2), 377-382, 1988
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