Ulug M. Unligil, Ph.D. - Publications
Affiliations: | 2002 | University of Toronto, Toronto, ON, Canada |
Area:
sturucture of glycosyltransferasesYear | Citation | Score | |||
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2001 | Chen W, Unligil UM, Rini JM, Stanley P. Independent Lec1A CHO glycosylation mutants arise from point mutations in N-acetylglucosaminyltransferase I that reduce affinity for both substrates. Molecular consequences based on the crystal structure of GlcNAc-TI. Biochemistry. 40: 8765-72. PMID 11467936 DOI: 10.1021/Bi015538B | 0.463 | |||
2000 | Unligil UM, Rini JM. Glycosyltransferase structure and mechanism. Current Opinion in Structural Biology. 10: 510-7. PMID 11042447 DOI: 10.1016/S0959-440X(00)00124-X | 0.491 | |||
2000 | Unligil UM, Zhou S, Yuwaraj S, Sarkar M, Schachter H, Rini JM. X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily. The Embo Journal. 19: 5269-80. PMID 11032794 DOI: 10.1093/Emboj/19.20.5269 | 0.547 | |||
1998 | Sarkar M, Pagny S, Unligil U, Joziasse D, Mucha J, Glössl J, Schachter H. Removal of 106 amino acids from the N-terminus of UDP-GlcNAc: alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I does not inactivate the enzyme. Glycoconjugate Journal. 15: 193-7. PMID 9557881 DOI: 10.1023/A:1006928624913 | 0.473 | |||
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