Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Chris Armishaw"'
Autor:
Hunt Je, Prue H. Hart, Jodie L. Simpson, Zheng Yang, Hong Cai, Paul F. Alewood, Nick Di Girolamo, J. Margaret Hughes, Nicodemus Tedla, Wei Xing Yan, Carolyn L. Geczy, Peter G. Gibson, Hong Wei Wang, Michael A. Perry, Chris Armishaw, T Hampartzoumian
Publikováno v:
Journal of Allergy and Clinical Immunology. 119:106-114
Background: The calcium-binding protein S100A12 might provoke inflammation and monocyte recruitment through the receptor for advanced glycation end products. Objective: Because inflammation elicited by S100A12 in vivo had characteristics of mast cell
Autor:
Chris Armishaw, Elizabeth Westbury, Catherine F. Latham, Jamie A. Lopez, Nia J. Bryant, Christine L. Gee, David E. James, Duncan H. Blair, Shu-Hong Hu, Paul F. Alewood, Jennifer L. Martin
Publikováno v:
Traffic. 7:1408-1419
Sec1p/Munc18 (SM) proteins are believed to play an integral role in vesicle transport through their interaction with SNAREs. Different SM proteins have been shown to interact with SNAREs via different mechanisms, leading to the conclusion that their
Autor:
Carolyn L. Geczy, Wei Xing Yan, Paul F. Alewood, Zheng Yang, Hong Cai, Jesse Goyette, Chris Armishaw
Publikováno v:
The Journal of biological chemistry. 283(19)
S100A12 is expressed at sites of acute, chronic, and allergic inflammation. S100 proteins have regions of high sequence homology, but the "hinge" region between the conserved calcium binding domains is structurally and functionally divergent. Because
Autor:
Chris Armishaw, Christine L. Gee, David E. James, Shu Hong Hu, Catherine F. Latham, Jennifer L. Martin, Paul F. Alewood
Publikováno v:
Acta crystallographica. Section F, Structural biology and crystallization communications. 63(Pt 6)
The production of diffraction-quality crystals of Munc18c, a protein involved in regulating vesicular exocytosis in mammals, is reported. The diffraction resolution of Munc18c crystals was optimized by (i) cocrystallizing with a peptide fragment of t
Publikováno v:
Australian Journal of Chemistry. 56:769
Conotoxins, a class of marine peptides rich in disulfide bonds, contain many of the structural elements present in larger proteins, such as α-helices and β-turns. In addition, these natural products are remarkably stable and exhibit exceptional rec