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1 d two beaded filament proteins (phakinin and filensin).
2 fiber cell: CP49 (phakinin) and CP115/CP95 (filensin).
3 in beta-B1-crystallin, Hsp-90, spectrin and filensin.
4 olytic N-acetylation and N-myristoylation of filensin.
5 sion of large quantities of MIP26, CP49, and filensin.
6 eta- and gamma-crystallins, MIP26, CP49, and filensin.
7 alysis of both CP49 and its assembly partner filensin.
8 ulted in the coprecipitation of phakinin and filensin.
10 d sites of phosphorylation and truncation in filensin and CP49 and revealed two unusual PTMs: postpro
12 copy, regions of colocalization of AQP0 with filensin and CP49 at the fiber cell plasma membrane in t
13 separated by SDS-PAGE, and the corresponding filensin and CP49 bands were digested by trypsin, Lys C,
15 filament network consisting of the proteins filensin and CP49, and it was recently reported that the
18 ajor intrinsic protein 26 (MIP26), CP49, and filensin and morphologic changes such as cell multilayer
23 ce were probed for the IF proteins phakosin, filensin, and vimentin, using light microscope immunocyt
25 ediate filament proteins phakinin (CP49) and filensin (CP115), and vimentin during a mild 20-minute h
40 nsin gene successfully blocked production of filensin mRNA, reduced levels of filensin's assembly par
41 at FVB/N mice do not have detectable CP49 or filensin protein in the lens, whereas C57BL/6 mice have
42 (residues 33-44), betaA4 (residues 106-117), filensin (residues 78-90), and phakinin (residues 77-89)
44 oduction of filensin mRNA, reduced levels of filensin's assembly partner CP49, and prevented the asse
45 e the protein levels of its assembly partner filensin, suggesting a mechanism for the regulation of b
46 termediate phenotype, showing a reduction in filensin transcript and moderate light-scattering at 5 m
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