Zobrazeno 1 - 10
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pro vyhledávání: '"Douglas, N.W."'
Autor:
Cooper, Douglas N.W. *
Publikováno v:
In BBA - General Subjects 2002 1572(2):209-231
Autor:
Douglas N.W. Cooper, Guillermo Giménez-Gallego, Antonio A. Romero, Hans-Joachim Gabius, María F. López-Lucendo
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 60:721-724
It is the aim of comparative structural biology to define the evolutionarily important traits of protein function and the points of diversification. Consequently, structural analysis, especially of distant members in a family which in this case are l
Autor:
Douglas N.W. Cooper
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1572:209-231
With the rapid explosion of genomic sequence databases, there has been an equivalent boom in genomics, the use of sequence information to define and compare gene families and their organization across diverse species. Such expansion of the galectin f
Autor:
Douglas N.W. Cooper
Publikováno v:
Trends in Glycoscience and Glycotechnology. 9:57-67
Autor:
Deborah Fowlis, Céline Colnot, Virginetta Cannon, Françoise Poirier, Marie-Anne Ripoche, Frédéric Scaerou, Douglas N.W. Cooper
Publikováno v:
Trends in Glycoscience and Glycotechnology. 9:31-40
ガレクチンはβ-ガラクトシドに特異的な糖認識分子のファミリーである。分子量が14から36kDaと小さく、細胞内の分布状況も様々であることから、他の動物レクチンとは区別される。現在
Autor:
Frédéric van den Brûle, Manuel Deprez, Douglas N.W. Cooper, Mark E. Sobel, Crina Buicu, Vincent Castronovo, Robert C. Bast, Claudette Pieters, Andrew Berchuck, Fu-Tong Liu
Publikováno v:
Human Pathology. 27:1185-1191
Alterations of tumor cell interactions with laminin, a basement membrane glycoprotein, are consistent features of the invasive and metastatic phenotype. Qualitative and quantitative changes in the expression of cell surface laminin-binding proteins h
Publikováno v:
The Journal of Cell Biology
Several physiologically important proteins lack a classical secretory signal sequence, yet they are secreted from cells. To investigate the secretion mechanism of such proteins, a representative mammalian protein that is exported by a nonclassical me
Publikováno v:
Journal of Biological Chemistry. 269:20807-20810
Publikováno v:
Biochemistry. 32:260-267
The soluble mammalian lactose-binding lectins L-14-I and L-29 are both secreted and bind to oligosaccharides on laminin, a large extracellular matrix glycoprotein containing polylactosamine chains. Because of the potential functional significance of
Publikováno v:
The Journal of Cell Biology
The Journal of cell biology, vol 115, iss 5
The Journal of cell biology, vol 115, iss 5
L-14, a dimeric lactose-binding lectin with subunits of 14 kD, is expressed in a wide range of vertebrate tissues. Several functions have been postulated for this lectin, but definitive evidence for a specific biological role has been elusive. In mus