Titlebook: Mammalian Carbohydrate Recognition Systems; Paul R. Crocker Book 2001 Springer-Verlag Berlin Heidelberg 2001 Oligosaccharid.cell.endoplasm

Limpid

The Man/GaINAc-4-SO4-Receptor has Multiple Specificities and Functions,glycoproteins in the endoplasmic reticulum (Helenius 1994; Williams 1995; Trombetta and Helenius 1998), transport of glycoproteins to lysosomes (Kornfeld 1990, 1992), control of the circulatory half-life of individual glycoproteins (Drickamer 1991; Baenziger et al. 1992; Drickamer and Taylor 1993),

Neuropeptides

用樹皮

Ligands for Siglecs,s have been found to occur in nature (Table 1). Their structure, occurrence and metabolic pathways have been reviewed in detail (Rosenberg 1995; Kelm and Schauer 1997; Schauer and Kamerling 1997; Varki 1997).

Irrepressible

Functions of Selectins,ons of the selectins require the N-terminal C-type lectin domain. The lectin domains show the highest degree of homology among different species (about 72% identity) and considerable homology among the three selectins within the same species (about 52% for human selectins; Kansas 1996). All three se

BOLUS

Carbohydrate Ligands for the Leukocyte-Endothelium Adhesion Molecules, Selectins,endothelium adhesion molecules (Brandley et al. 1990; Harlan et al. 1992; Bevilacqua et al. 1993). As discussed by Dr Klaus Ley (this volume), the three molecules are key players in mechanisms of innate immunity, for they have important roles at the initial stages of recruitment and emigration of le

事情

Structures and Functions of Mammalian Collectins,cognition and cell-pathogen interactions using structurally related calcium-dependent carbohydrate recognition domains (C-type CRDs). The collectins are a group of mammalian lectins containing collagen regions. They include mannose-binding lectin (MBL), lung surfactant protein A (SP-A), lung surfact

Hirsutism

苦澀

Results and Problems in Cell Differentiationhttp://image.papertrans.cn/m/image/622030.jpg

forthy

Feedback

Lectins of the ER Quality Control Machinery,, this protein has been shown to belong to a new family of chaperones or proteins with lectin-like properties with orthologs present in all eukaryotes so far studied (Wada et al. 1991; Hebert et al. 1995). Calnexin and calreticulin, an ER luminal homologue, share extensive sequence similarity and both bind calcium.