Zobrazeno 1 - 10
of 14
pro vyhledávání: '"J H Grubb"'
Autor:
Lee J. Helman, Yeo Kyoung Oh, H. L. Muller, William S. Sly, Caterina P. Minniti, Elise C. Kohn, J. H. Grubb, R. G. Rosenfeld
Publikováno v:
Journal of Biological Chemistry. 267:9000-9004
Insulin-like growth factor-II (IGF-II) is an autocrine growth and motility factor for human rhabdomyosarcoma. It interacts with three different receptors: the IGF-I, the IGF-II, and the insulin receptor. A specific function of the IGF-II receptor in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::388558c7a953f17ad3cec03bcd7cd37d
https://doi.org/10.1016/s0021-9258(19)50379-9
https://doi.org/10.1016/s0021-9258(19)50379-9
Autor:
Yoshitake Murayama, Tetsuji Okamoto, W S Sly, Toshiaki Katada, Etsuro Ogata, J H Grubb, Ikuo Nishimoto, M Ui, T. Iiri, Tomoichiro Asano
Publikováno v:
Journal of Biological Chemistry. 265:17456-17462
The rat insulin-like growth factor II (IGF-II) receptor develops transmembrane signaling functions by directly coupling to a guanine nucleotide-binding protein (G protein) having a 40-kDa alpha subunit, Gi-2, whereas recent studies have indicated tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dec765746ebd68f16a3ed9ee39e51d83
https://doi.org/10.1016/s0021-9258(18)38185-7
https://doi.org/10.1016/s0021-9258(18)38185-7
Autor:
S. Tomatsu, K. Okamura, H. Maeda, T. Taketani, S. V. Castrillon, M. A. Gutierrez, T. Nishioka, A. A. Fachel, K. O. Orii, J. H. Grubb, A. Cooper, M. Thornley, E. Wraith, L. A. Barrera, L. S. Laybauer, R. Giugliani, I. V. Schwartz, G. Schulze Frenking, M. Beck, S. G. Kircher, E. Paschke, S. Yamaguchi, K. Ullrich, M. Haskins, K. Isogai, Y. Suzuki, T. Orii, N. Kondo, M. Creer, T. Okuyama, A. Tanaka, A. Noguchi
Publikováno v:
Journal of inherited metabolic disease. 28(2)
The mucopolysaccharidoses (MPS) is characterized by accumulation of glycosaminoglycans (GAGs), and mucolipidosis (ML) by accumulation of GAGs and sphingolipids. Each type of MPS accumulates specific GAGs. The lysosomal enzymes N-acetylgalactosamine-6
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b388f86aa4f6c43555a54d651f4c82bf
https://pubmed.ncbi.nlm.nih.gov/15877208
https://pubmed.ncbi.nlm.nih.gov/15877208
Publikováno v:
The Journal of biological chemistry. 274(33)
Human beta-glucuronidase (hGUSB) is a member of family 2 glycosylhydrolases that cleaves beta-D-glucuronic acid residues from the nonreducing termini of glycosaminoglycans. Amino acid sequence and structural homology of hGUSB and Escherichia coli bet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7ce1c0fb80560a56ff6a1cf3f6a1a94b
https://pubmed.ncbi.nlm.nih.gov/10438523
https://pubmed.ncbi.nlm.nih.gov/10438523
Publikováno v:
The Journal of biological chemistry. 268(30)
beta-Glucuronidase undergoes proteolytic C-terminal processing during or after its transport to lysosomes or endosomes. We determined the C-terminal processing site for human placental beta-glucuronidase to be the peptide bond between Thr633-Arg634.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dc9de09e812d24f05fb5f6b23043531d
https://pubmed.ncbi.nlm.nih.gov/8226771
https://pubmed.ncbi.nlm.nih.gov/8226771
Publikováno v:
The Journal of biological chemistry. 268(16)
Phosphorylation of mannose residues on N-linked oligosaccharide side chains of lysosomal enzymes targets them to lysosomes. We used site-directed mutagenesis to observe the effect of eliminating selective glycosylation sites from human beta-glucuroni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b1c9ab045336d7cbcaf55d077933d266
https://pubmed.ncbi.nlm.nih.gov/8505339
https://pubmed.ncbi.nlm.nih.gov/8505339
Publikováno v:
American journal of human genetics. 52(3)
PCR of cDNA produced from patient fibroblasts allowed us to determine the paternal mutation in the first patient reported with beta-glucuronidase-deficiency mucopolysaccharidosis type VII (MPS VII). The G-->T transversion 1,881 bp downstream of the A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::506d822c12714ce98ce6a2df46f13ed7
https://pubmed.ncbi.nlm.nih.gov/7680524
https://pubmed.ncbi.nlm.nih.gov/7680524
Publikováno v:
The Journal of biological chemistry. 267(26)
The quaternary structure and binding activity of the murine 46-kDa mannose 6-phosphate receptor (46MPR) were studied in semi-intact murine cells that overexpress the murine receptor. Chemical cross-linking studies showed that the murine 46MPR exists
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::19faeea6a3ecbe0299acda5b161b21d8
https://pubmed.ncbi.nlm.nih.gov/1326539
https://pubmed.ncbi.nlm.nih.gov/1326539
Autor:
C P, Minniti, E C, Kohn, J H, Grubb, W S, Sly, Y, Oh, H L, Müller, R G, Rosenfeld, L J, Helman
Publikováno v:
The Journal of biological chemistry. 267(13)
Insulin-like growth factor-II (IGF-II) is an autocrine growth and motility factor for human rhabdomyosarcoma. It interacts with three different receptors: the IGF-I, the IGF-II, and the insulin receptor. A specific function of the IGF-II receptor in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8ec5d85b8696d30c4b3b644c2f00aa39
https://pubmed.ncbi.nlm.nih.gov/1315746
https://pubmed.ncbi.nlm.nih.gov/1315746
Publikováno v:
The Journal of biological chemistry. 266(16)
We have cloned and sequenced the 2175-nucleotide, full-length cDNA for the mouse 46-kDa Man 6-P receptor (46MPR) and studied its functional properties in stably transfected mouse L cells which do not express the insulin-like growth factor-II receptor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f401a81268f524cbf47ad42d4d86c82d
https://pubmed.ncbi.nlm.nih.gov/1645352
https://pubmed.ncbi.nlm.nih.gov/1645352