VIP36Vesicular Integral Protein of 36 Kilodaltons (intracellular animal lectin)
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(2008) Molecular basis of sugar recognition by the human L-type lectins ERGIC-53, VIPL, and VIP36. J.
The results clearly showed that ERGIC-53 co-precipitated with VIPL, but not with VIP36, and that the ERGIC-53-VIPL interaction is mediated by the transmembrane or cytoplasmic domains of these cargo receptors (Fig.
VIP36 preferentially recognizes deglucosylated A-arms and delivers N-glycan-unprocessed glycoproteins (which may be misfolded) from the Golgi to the ER, where the chaperone BiP enhances correct folding.
(2007) Detection of weak sugar binding activity of VIP36 using VIP36-streptavidin complex and membrane-based sugar chains.
(2007) Stable interaction of the cargo receptor VIP36 with molecular chaperone BiP.