Michael N.G. James
Affiliations: | Biochemistry | University of Alberta, Edmonton, Alberta, Canada |
Area:
protein crystallographyWebsite:
http://biochem.med.ualberta.ca/Research/faculty/Professors/Pages/James.aspxGoogle:
"Michael N.G. James"Bio:
http://www.amercrystalassn.org/documents/newsletterarchive/2008Winter.pdf
Mean distance: 8.13 | S | N | B | C | P |
Cross-listing: Crystallography Tree
Children
Sign in to add trainee| Jason Maynes | grad student | (Crystallography Tree) | |
| Natalie Strynadka | grad student | 1990 | University of Alberta |
| Nina K. Bernstein | grad student | 2000 | University of Alberta (Canada) |
| Isabelle Barrette-Ng | grad student | 2003 | University of Alberta (Canada) |
| Brian L. Mark | grad student | 2003 | University of Alberta (Canada) |
| Bernard D Santarsiero | post-doc | 1986-1990 | University of Alberta |
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Publications
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| Liu Y, Guardia-Laguarta C, Yin J, et al. (2017) The Ubiquitination of PINK1 Is Restricted to Its Mature 52-kDa Form. Cell Reports. 20: 30-39 |
| Baral PK, Swayampakula M, Aguzzi A, et al. (2015) X-ray structural and molecular dynamical studies of the globular domains of cow, deer, elk and Syrian hamster prion proteins. Journal of Structural Biology. 192: 37-47 |
| Baral PK, Swayampakula M, Rout MK, et al. (2014) Structural basis of prion inhibition by phenothiazine compounds. Structure (London, England : 1993). 22: 291-303 |
| Jacobson JM, Yin J, Kitov PI, et al. (2014) The crystal structure of shiga toxin type 2 with bound disaccharide guides the design of a heterobifunctional toxin inhibitor. The Journal of Biological Chemistry. 289: 885-94 |
| Baral P, Swayampakula M, Rout M, et al. (2014) Structural Basis of Prion Protein Conformation Conversion Inhibition Acta Crystallographica Section a Foundations and Advances. 70: C812-C812 |
| Bie H, Yin J, He X, et al. (2013) Insights into mucopolysaccharidosis I from the structure and action of α-L-iduronidase. Nature Chemical Biology. 9: 739-45 |
| Jacob-Ferreira AL, Kondo MY, Baral PK, et al. (2013) Phosphorylation status of 72 kDa MMP-2 determines its structure and activity in response to peroxynitrite. Plos One. 8: e71794 |
| Sonati T, Reimann RR, Falsig J, et al. (2013) The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein. Nature. 501: 102-6 |
| Swayampakula M, Baral PK, Aguzzi A, et al. (2013) The crystal structure of an octapeptide repeat of the prion protein in complex with a Fab fragment of the POM2 antibody. Protein Science : a Publication of the Protein Society. 22: 893-903 |
| Skene-Arnold TD, Luu HA, Uhrig RG, et al. (2013) Molecular mechanisms underlying the interaction of protein phosphatase-1c with ASPP proteins. The Biochemical Journal. 449: 649-59 |