Michael W. Parker
St. Vincent's Institute of Medical Research
496 Papers
4.8K Citations
Michael W. Parker is an academic researcher from St. Vincent's Institute of Medical Research. The author has contributed to research in topics: Biology & Chemistry. The author has an hindex of 78, co-authored 473 publications. Previous affiliations of Michael W. Parker include Centre national de la recherche scientifique & Monash University.
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Papers
Origin of the West Nile Virus Responsible for an Outbreak of Encephalitis in the Northeastern United States
Robert S. Lanciotti,John T. Roehrig,Vincent Deubel,Jonathan D. Smith,Michael W. Parker,K. Steele,B. Crise,K. E. Volpe,Mary B. Crabtree,Jacqueline H. Scherret,Roy A. Hall,John S. Mackenzie,C. B. Cropp,B. Panigrahy,Eileen N. Ostlund,B. Schmitt,M. Malkinson,C. Banet,Joel S. Weissman,Nicholas Komar,Harry M. Savage,Ward B. Stone,Tim McNamara,Duane J. Gubler +23 more
TL;DR: In late summer 1999, an outbreak of human encephalitis occurred in the northeastern United States that was concurrent with extensive mortality in crows (Corvus species) as well as the deaths of several exotic birds at a zoological park in the same area.
1.6K
Pore-forming protein toxins: from structure to function.
TL;DR: Recent work suggests a number of common features in the mechanism of membrane insertion may exist for each class of PFTs, and nearly all can be classified into one of two families based on the types of pores they are thought to form: alpha-P FTs or beta-PFTs.
490
AMPK β Subunit Targets Metabolic Stress Sensing to Glycogen
Galina Polekhina,Abhilasha Gupta,Belinda J. Michell,Bryce J. W. van Denderen,Sid Murthy,Susanne C. Feil,Ian G. Jennings,Duncan J. Campbell,Duncan J. Campbell,Lee A. Witters,Michael W. Parker,Michael W. Parker,Bruce E. Kemp,Bruce E. Kemp,David Stapleton,David Stapleton +15 more
TL;DR: It is shown that the AMPK β subunit contains a functional glycogen binding domain (β-GBD) that is most closely related to isoamylase domains found in glycogen and starch branching enzymes.
440
Mechanism of Activation of Protein Kinase JAK2 by the Growth Hormone Receptor
Andrew J. Brooks,Wei Dai,Megan L. O'Mara,Daniel Abankwa,Yash Chhabra,Rebecca A. Pelekanos,Olivier Gardon,Kathryn A. Tunny,Kristopher M. Blucher,Craig J. Morton,Michael W. Parker,Michael W. Parker,Emma Sierecki,Yann Gambin,Guillermo A. Gomez,Kirill Alexandrov,Ian A. Wilson,Manolis Doxastakis,Alan E. Mark,Michael J. Waters +19 more
TL;DR: The mechanism provides a molecular basis for understanding the oncogenic JAK2 mutations responsible for polycythemia vera and certain other hematologic disorders and may thus be of value in the design of small-molecule inhibitors of clinical applicability.