Kinetic Analysis of L1 Homophilic Interaction
نویسندگان
چکیده
منابع مشابه
Kinetic analysis of L1 homophilic interaction: role of the first four immunoglobulin domains and implications on binding mechanism.
L1 is a cell adhesion molecule of the immunoglobulin (Ig) superfamily, critical for central nervous system development, and involved in several neuronal biological events. It is a type I membrane glycoprotein. The L1 ectodomain, composed of six Ig-like and five fibronectin (Fn) type-III domains, is involved in homophilic binding. Here, co-immunoprecipitation studies between recombinant truncate...
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A new mouse line has been produced in which the sixth Ig domain of the L1 cell adhesion molecule has been deleted. Despite the rather large deletion, L1 expression is preserved at normal levels. In vitro experiments showed that L1-L1 homophilic binding was lost, along with L1-alpha5beta1 integrin binding. However, L1-neurocan and L1-neuropilin binding were preserved and sema3a responses were in...
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The molecular pathogenesis of many Staphylococcus aureus infections involves growth of bacteria as biofilm. In addition to polysaccharide intercellular adhesin (PIA) and extracellular DNA, surface proteins appear to mediate the transition of bacteria from planktonic growth to sessile lifestyle as well as biofilm growth, and can enable these processes even in the absence of PIA expression. Howev...
متن کاملAdditional Data File 1 Homophilic Interaction of Unc-69
unc-69(ok339) deletion unc-69(ok339) deletes a 2.65 kb genomic fragment encompassing the whole unc-69 transcription unit as well as flanking sequences both 5’ and 3’ of the gene (Supplemental Figure S1). Thus, this deletion is certain to represent a null allele of unc-69. unc-69(ok339) homozygotes have an Unc phenotype and arrest during L1 to L2 transition (Supp. Table S2). We found that ok339 ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2008
ISSN: 0021-9258
DOI: 10.1074/jbc.m804991200