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pro vyhledávání: '"Birgit Zipser"'
Autor:
Birgit Zipser
Publikováno v:
Neuronal Factors ISBN: 9780429277634
Neuronal Factors
Neuronal Factors
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f0574d91141b8eb5bc9e24cccc2dd004
https://doi.org/10.1201/9780429277634-6
https://doi.org/10.1201/9780429277634-6
Autor:
Birgit Zipser, Carol Schley
Publikováno v:
Neuronal Factors ISBN: 9780429277634
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2b0dd0581fd3c0aa25990649cd77862b
https://doi.org/10.1201/9780429277634-5
https://doi.org/10.1201/9780429277634-5
Publikováno v:
Development Genes and Evolution. 220:77-87
The biological function of a cell-type-specific glycosylation of an adhesion molecule belonging to the L1CAM immunoglobulin superfamily was previously determined in the nervous system of the embryonic leech, Hirudo medicinalis. The Lan3-2 glycoepitop
Autor:
Rawle I. Hollingsworth, Birgit Zipser, Anne Dell, Stuart M. Haslam, Howard R. Morris, Linjuan Huang
Publikováno v:
Journal of Neurochemistry. 107:1448-1456
While glycosyltransferases are restrictively expressed in invertebrate model organisms, little is known of their glycan end products. One such restrictively expressed glycoepitope was localized to sensory and epithelial cells of leech and Caenorhabdi
Autor:
John Jellies, Deepa V. Venkitaramani, Kristen M. Johansen, Dong Wang, Yun Ji, Ying Zhi Xu, Liliana Ponguta, Jørgen Johansen, Birgit Zipser, Katie Bock
Publikováno v:
Journal of Neurobiology. 60:369-380
The Lan3-14 and Laz10-1 monoclonal antibodies recognize a 400 kDa antigen that is specifically expressed by all muscle cells in leech. We show that the antigen recognized by both antibodies is a member of the filamin family of actin binding proteins.
Publikováno v:
Journal of Biological Chemistry. 278:4322-4330
Tractin is a member of the L1 family of cell adhesion molecules in leech. Immunoblot analysis suggests that Tractin is constitutively cleaved in vivo at a proteolytic site with the sequence RKRRSR. This sequence conforms to the consensus sequence for
Autor:
Robert N. Cole, Birgit Zipser
Publikováno v:
Journal of Neurochemistry. 63:75-85
Leech lectin 35 (LL35) is a calcium-independent galactoside-binding protein with a molecular mass of 35 kDa and binding properties similar to those of calcium-independent, galactose-specific lectins found in vertebrates, sponges, and nematodes. LL35
Autor:
Birgit Zipser, Robert N. Cole
Publikováno v:
Journal of Neurochemistry. 63:66-74
Three lactose-binding proteins with apparent molecular masses of 16, 35, and 63 kDa [leech lectin 16, 35, and 63 (LL,16, LL35, and LL63, respectively)] were isolated from leech membranes. Polyclonal antibodies raised against LL35 cross-reacted with L
Autor:
Birgit Zipser, Mei Hui Tai
Publikováno v:
Journal of Neurocytology. 31:743-754
Differences in carbohydrate signaling control sequential steps in synaptic growth of sensory afferents in the leech. The relevant glycans are constitutive and developmentally regulated modifications of leechCAM and Tractin (family members of NCAM and
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1452(2):161-171
LeechCAM is a recently described member of the Ig-superfamily which has five Ig-domains, two FNIII-domains, a transmembrane domain, and a cytoplasmic domain. Phylogenetic analysis indicated that LeechCAM is the leech homolog of apCAM, FasII, and vert