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1 membrane proteins together with PAGFP-tagged clathrin light chain.
2 ed alone or with photoactivatable GFP-tagged clathrin light chain.
3 or the S3 path as an interaction surface for clathrin light chain.
4 ) that includes residues crucial for binding clathrin light chain.
5 ith clathrin-mediated endocytosis, including clathrin light chain.
6 r interaction with the conserved sequence of clathrin light chains.
7 avy chain subunits nor bind significantly to clathrin light chains.
8 isms, as well as Retinitis Pigmentosa Type 2-Clathrin Light Chain, a membrane protein with a novel do
10 ns of beta-actin, occludin, claudin-1, ZO-1, clathrin light chain A1, and caveolin-1 were imaged by t
12 re clathrin-mediated endocytosis and labeled clathrin light chain also displayed altered localization
15 ating with slightly different affinities for clathrin light chain and more markedly with effects of c
16 =200 nm clusters of transferrin receptor and clathrin light chain at < or =25 nm resolution and confi
17 thrin-coated vesicles and to colocalize with clathrin light chain at putative sites of endocytosis at
18 n overlaps the domain putatively involved in clathrin light chain binding and is adjacent to the heav
20 ight chain and more markedly with effects of clathrin light chain binding on Hip protein-actin intera
23 dynamin K44A, epsin 2a, amphiphysin A1, and clathrin light chain but enhanced by that for the active
24 Expression of FK506 binding protein (FKBP)-clathrin light chain chimeras, to inhibit clathrin membr
25 icle is the clathrin triskelion, composed of clathrin light chain (Clc) and clathrin heavy chain (Chc
34 in CLC1-knockout yeast, which indicates that clathrin light chain facilitates the transition from the
35 tic perturbation of clathrin function with a clathrin light chain-FKBP chimera oligomerizable by the
36 at the cell cortex, which colocalized with a clathrin light chain fluorescent fusion protein (CLC-FFP
39 pits labeled with green fluorescent protein-clathrin light chains in HeLa cells show that even when
41 t, real-time analysis of Hip1R-YFP and DsRed-clathrin light chain (LC) in live cells revealed that th
45 us does not appear to colocalize with either clathrin light chain or caveolin-1 by immunofluorescence
46 croscopy using fluorescent proteins fused to clathrin light chain or GLUT4 reveals these structures a
49 ents of the clathrin heavy chain, which bind clathrin light-chain subunits and mimic the self-assembl
52 foci overlap with those formed by DRP1C and clathrin light chain, there are clear differences in beh
53 ows the observed conformational variation in clathrin light chains to alter the conformation of the c
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