Zobrazeno 1 - 10
of 32
pro vyhledávání: '"William M. Canfield"'
Autor:
Hua Li, Wang-Sik Lee, Xiang Feng, Lin Bai, Benjamin C. Jennings, Lin Liu, Balraj Doray, William M. Canfield, Stuart Kornfeld, Huilin Li
Publikováno v:
Nat Struct Mol Biol
Vertebrates utilize the mannose 6-phosphate (M6P) recognition system to deliver lysosomal hydrolases to lysosomes. Key to this pathway is GlcNAc-1-phosphotransferase (PTase) that selectively adds GlcNAc-P to mannose residues of the hydrolases. Human
Autor:
Yi Qian, Peter Lobel, Mariko Kudo, Stuart Kornfeld, Meiqian Qian, Wang Sik Lee, William M. Canfield, Intaek Lee
Publikováno v:
Journal of Biological Chemistry. 285:3360-3370
UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase is an alpha(2)beta(2)gamma(2) hexamer that mediates the first step in the synthesis of the mannose 6-phosphate recognition marker on lysosomal acid hydrolases. Using a multifaceted
Autor:
Richard N. Bohnsack, Richard D. Cummings, Nancy M. Dahms, Xuezheng Song, Russell Gotschall, Mariko Kudo, Linda J. Olson, David F. Smith, William M. Canfield
Publikováno v:
Journal of Biological Chemistry. 284:35215-35226
The 300-kDa cation-independent mannose 6-phosphate receptor (CI-MPR), which contains multiple mannose 6-phosphate (Man-6-P) binding sites that map to domains 3, 5, and 9 within its 15-domain extracytoplasmic region, functions as an efficient carrier
Publikováno v:
Journal of Biological Chemistry. 280:36141-36149
Lysosomal enzymes are targeted to the lysosome through binding to mannose 6-phosphate receptors because their glycans are modified with mannose 6-phosphate. This modification is catalyzed by UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamin
Autor:
Valarie L. Tlapak-Simmons, Christina A. Baron, William M. Canfield, Paul H. Weigel, Russell Gotschall, Dewan Haque
Publikováno v:
Journal of Biological Chemistry. 280:13012-13018
Previous studies reached different conclusions about whether class I hyaluronan synthases (HASs) elongate hyaluronic acid (HA) by addition to the reducing or the nonreducing end. Here we used two strategies to determine the direction of HA synthesis
Autor:
William M. Canfield, Karen L. Lee, Tim Edmunds, Kevin Brewer, Rodney J. Moreland, Roger W. Decker, Robert D. Cauthron, Karen L. Albee, X. Kate Zhang, Xiaoying Jin
Publikováno v:
Journal of Biological Chemistry. 280:6780-6791
Pompe's disease is caused by a deficiency of the lysosomal enzyme acid alpha-glucosidase (GAA). GAA is synthesized as a 110-kDa precursor containing N-linked carbohydrates modified with mannose 6-phosphate groups. Following trafficking to the lysosom
Publikováno v:
Journal of Biological Chemistry. 277:29737-29744
N-Acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase, also known as "uncovering" enzyme (UCE), is localized in the trans-Golgi network, where it removes a covering N-acetylglucosamine from the mannose 6-phosphate recognition marker on l
Publikováno v:
Journal of Biological Chemistry. 277:169-177
The O-linked oligosaccharides (O-glycans) in mammalian glycoproteins are classified according to their core structures. Among the most common is the core 1 disaccharide structure consisting of Galbeta1--3GalNAcalpha1--Ser/Thr, which is also the precu
Autor:
Ming Bao, Kevin Brewer, Annick Raas-Rothschild, William M. Canfield, Rémi Salomon, Arnold Munnich, Valérie Cormier-Daire, Emmanuelle Génin, Marsha Zeigler, Hanna Mandel, Steve Toth, Bruce A. Roe
Publikováno v:
Journal of Clinical Investigation. 105:673-681
Mucolipidosis IIIC, or variant pseudo-Hurler polydystrophy, is an autosomal recessive disease of lysosomal hydrolase trafficking. Unlike the related diseases, mucolipidosis II and IIIA, the enzyme affected in mucolipidosis IIIC (N-Acetylglucosamine-1
Publikováno v:
Journal of Biological Chemistry. 274:32778-32785
We have isolated and sequenced human cDNA and mouse genomic DNA clones encoding N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase (phosphodiester alpha-GlcNAcase) which catalyzes the second step in the synthesis of the mannose 6-phos