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Biochemistry|October 23, 1997
Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cellsB Hazes, R J ReadJournal of Molecular Biology|May 17, 1996
Crystal structure of the pertussis toxin-ATP complex: a molecular sensorB Hazes, A Boodhoo, S A Cockle, et al.Journal of Molecular Biology|June 14, 2000
Crystal structure of Pseudomonas aeruginosa PAK pilin suggests a main-chain-dominated mode of receptor bindingB Hazes, P A Sastry, K Hayakawa, et al.The EMBO Journal|June 1, 1997
Aerolysin and pertussis toxin share a common receptor-binding domainJ Rossjohn, J T Buckley, B Hazes, et al.Journal of Molecular Biology|November 2, 1999
A 2.6 A structure of a serpin polymer and implications for conformational diseaseJ A Huntington, N S Pannu, B Hazes, et al.Biochemistry|March 4, 1998
Structure of the shiga-like toxin I B-pentamer complexed with an analogue of its receptor Gb3H Ling, A Boodhoo, B Hazes, et al.Protein Science : a Publication of the Protein Society|August 1, 1996
The (QxW)3 domain: a flexible lectin scaffoldB HazesProceedings of the National Academy of Sciences of the United States of America|January 5, 2000
Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational diseaseB Gooptu, B Hazes, W S Chang, et al.Proteins|March 1, 1992
Comparison of the hemocyanin beta-barrel with other Greek key beta-barrels: possible importance of the "beta-zipper" in protein structure and foldingB Hazes, W G HolProtein Engineering|July 1, 1988
Model building of disulfide bonds in proteins with known three-dimensional structureB Hazes, B W DijkstraPageof 7