Zobrazeno 1 - 10
of 29
pro vyhledávání: '"J R Gum"'
Publikováno v:
Annals of Oncology. 10:S51-S55
Mucins are high molecular weight glycoproteins which are heavily glycosylated with many carbohydrate side chains. In epithelial cancers such as biliopancreatic cancer, both quantitative and qualitative alterations in carbohydrate and polypeptide moie
Autor:
J. R. Gum
Publikováno v:
Biochemical Society Transactions. 23:795-799
It has been clear for some time now that mucin glycoproteins have extensive, highly glycosylated tandem repeat domains. What is becoming increasingly apparent, however, is the diversity of unique sequences present on different mucins. Variations in m
Autor:
J R, Gum, J W, Hicks, A M, Gillespie, J L, Rius, P A, Treseler, S C, Kogan, E J, Carlson, C J, Epstein, Y S, Kim
Publikováno v:
Cancer research. 61(8)
Mucinous colorectal cancers exhibit a characteristic set of molecular genetic alterations and may be derived from progenitor cells committed to the goblet cell lineage. Previously, we demonstrated that the MUC2 mucin gene promoter drives transgene re
Autor:
D M, Swallow, L E, Vinall, J R, Gum, Y S, Kim, H, Yang, J I, Rotter, M, Mirza, J C, Lee, J E, Lennard-Jones
Publikováno v:
Journal of medical genetics. 36(11)
Publikováno v:
Annals of oncology : official journal of the European Society for Medical Oncology. 10
Mucins are high molecular weight glycoproteins which are heavily glycosylated with many carbohydrate side chains. In epithelial cancers such as biliopancreatic cancer, both quantitative and qualitative alterations in carbohydrate and polypeptide moie
Publikováno v:
The Biochemical journal. 338
Hepatocyte nuclear factor 1 was identified as the transcription factor binding to a 20 bp (-150 to -131) region of the gene for human dipeptidyl peptidase IV, which has been shown to be important for the expression of dipeptidyl peptidase IV in the h
Autor:
J R, Gum, J J, Ho, W S, Pratt, J W, Hicks, A S, Hill, L E, Vinall, A M, Roberton, D M, Swallow, Y S, Kim
Publikováno v:
The Journal of biological chemistry. 272(42)
MUC3 is a large mucin glycoprotein expressed by the human intestine and gall bladder. In this manuscript, we present details of the deduced protein structure of MUC3. The MUC3 carboxyl-terminal domain is 617 residues in length, including 511 residues
Publikováno v:
The Journal of biological chemistry. 272(26)
The distribution of MUC6 suggests that its primary function is protection of vulnerable epithelial surfaces from damaging effects of constant exposure to a wide range of endogenous caustic or proteolytic agents. A combination of genomic, cDNA. and 3'
Publikováno v:
The Journal of biological chemistry. 269(27)
To obtain cDNAs for analysis of mucin gene transcription in rat models of human disease, we screened a rat intestinal cDNA library in lambda ZAPII using an upstream non-tandem repeat cDNA fragment of the human MUC 2 gene (Gum, J., Hicks, J., Toribara
Publikováno v:
The Journal of biological chemistry. 269(4)
Secretory mucins consist of a protein backbone that is catenated by disulfide bonds, heavily O-glycosylated, and packaged into storage granules prior to release from cells. In this paper, we identify and sequence cDNAs that encode the amino terminus