In vitro studies on the assembly properties of the lens proteins CP49, CP115: coassembly with alpha-crystallin but not with vimentin.
about
Morphological characterization of the Alpha A- and Alpha B-crystallin double knockout mouse lensTargeted disruption of the mouse alpha A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha B-crystallinAltered aggregation properties of mutant gamma-crystallins cause inherited cataractThe cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro.Characterization of covalent multimers of crystallins in aging human lenses.A role for endogenous TGFalpha and associated signaling pathways in the differentiation of lens fiber cells.Distribution of bovine and rabbit lens alpha-crystallin products by MALDI imaging mass spectrometryRemoval of Hsf4 leads to cataract development in mice through down-regulation of gamma S-crystallin and Bfsp expression.Age-related changes in the spatial distribution of human lens alpha-crystallin products by MALDI imaging mass spectrometry.The eye lens cytoskeleton.Posttranslational modifications of the bovine lens beaded filament proteins filensin and CP49.Real-time observation of coiled-coil domains and subunit assembly in intermediate filaments.alpha-Crystallin chaperone-like activity and membrane binding in age-related cataracts.Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts.Characterization of the linker 2 region in human vimentin using site-directed spin labeling and electron paramagnetic resonance.Characterization of structural changes in vimentin bearing an epidermolysis bullosa simplex-like mutation using site-directed spin labeling and electron paramagnetic resonance.Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.Gene structure and cDNA sequence identify the beaded filament protein CP49 as a highly divergent type I intermediate filament protein.The genetics of cataract: our vision becomes clearer.Understanding the α-crystallin cell membrane conjunction.A transgenic mouse model for human autosomal dominant cataractEvolution of the vertebrate beaded filament protein, Bfsp2; comparing the in vitro assembly properties of a "tailed" zebrafish Bfsp2 to its "tailless" human orthologueProtein-protein interactions between lens vimentin and alphaB-crystallin using FRET acceptor photobleaching.Insights into the beaded filament of the eye lens.Identification of a novel CRYAB mutation associated with autosomal recessive juvenile cataract in a Saudi familyLens intermediate filamentsFunctions of the intermediate filament cytoskeleton in the eye lens.Lens Biology and BiochemistryAlterations in lenticular proteins during ageing and selenite-induced cataractogenesis in Wistar rats.Tropospheric ozone: an emerging environmental stress to skin.The function of filensin and phakinin in lens transparency.Interactive sequences in the stress protein and molecular chaperone human alphaB crystallin recognize and modulate the assembly of filamentsTreatment of keratin intermediate filaments with sulfur mustard analogs.Structural characterization of human vimentin rod 1 and the sequencing of assembly steps in intermediate filament formation in vitro using site-directed spin labeling and electron paramagnetic resonance.Head and rod 1 interactions in vimentin: identification of contact sites, structure, and changes with phosphorylation using site-directed spin labeling and electron paramagnetic resonance.Novel recessive BFSP2 and PITX3 mutations: insights into mutational mechanisms from consanguineous populations.Identification of a direct Aquaporin-0 binding site in the lens-specific cytoskeletal protein filensin.
P2860
Q24798190-07B6499E-2A6D-4750-86AF-6437A9494615Q28511428-D4AE26F2-796B-4EB1-9BD1-82C6CA49771EQ28589540-93B0CB5C-758B-4FC9-B3D4-6C01AC85ED0DQ30323290-6C9F62BE-82E5-459C-B070-28D97D517882Q31026778-C9CBA965-AC48-4D4B-BC08-962E4ACF31F8Q31909427-7879AFB7-1920-4EC9-8F6F-6A25F709A731Q33323349-E02B5AE6-685A-4661-99AB-756F9B4AC952Q33410189-D1484BFF-8F90-4381-8CE6-7F8BAE99C56FQ33433847-98721E07-8D31-4822-B2C6-28626AADC95EQ33812590-033FEEA9-7D43-46FB-A488-24556C27B5A3Q33845202-225ECFA0-3E87-41B3-B44A-B1552CFB64D2Q33966730-A6C22E6F-B5FB-4DFF-8A41-2C0F98A74D86Q33989116-2D67B6CC-A902-46D3-9839-6C059D3E03F9Q33989123-42F1EADC-2C84-48E2-B981-EC70836F768CQ33989279-4F19823A-16E2-4F20-913A-34225CD12C89Q33996864-71438B65-B4BA-4B70-80B3-4EF263921984Q34288930-5F6504C9-D99F-496E-9C88-F0BE4E5961BDQ34380467-072BDBC5-F7AD-4485-AB0B-F3E364977D6EQ34384832-2B44FBF7-A4E7-41D8-8243-729C9A6FA6BFQ35633311-7A29D1C5-17EE-4B01-B5AD-E98E0425D258Q35757577-6FBCA033-8C5A-493E-803B-6BD02F157C3FQ36670588-EFC59E8A-74B7-43C2-9119-A0E61B362545Q36749471-BED3997F-FDA1-4B8C-B123-053BEC9FC281Q36816245-EFC65BDD-CE0E-4600-BBB5-064D74272AC0Q37198218-409BDADF-00AA-4CD8-888D-3C1B80AACAF8Q37227723-A1B76092-B085-464A-8294-0A68CBC19B0BQ37545190-26B6E674-176E-47D0-A802-075217C19EEFQ38574368-1AEDEF4C-305D-4462-A838-CEC13251FC45Q39626993-E4305F6C-2C0D-43FE-8B7E-18721CC24FBBQ41679340-806D59CA-78D2-455B-9F71-08DC1D5B603EQ41844304-68A9AAAA-2A62-4AB8-8800-175B030A2DF5Q42058804-6EDBCEA5-DD25-46FB-B4B9-9B74E3BE95D4Q42085351-3CC49881-8F80-4194-B272-60E2EC3A60A7Q42734147-F55E5A95-CB45-4E6D-A84E-3BB0570B50BCQ42736271-989D76AD-455C-40BA-902A-CB37C69EDE36Q46690149-9E4B896E-265B-471D-B61B-AEC69CB16885Q51111833-8F7329E4-E248-44AB-8792-3518FBD8D812
P2860
In vitro studies on the assembly properties of the lens proteins CP49, CP115: coassembly with alpha-crystallin but not with vimentin.
description
1995 nî lūn-bûn
@nan
1995 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
In vitro studies on the assemb ...... stallin but not with vimentin.
@ast
In vitro studies on the assemb ...... stallin but not with vimentin.
@en
In vitro studies on the assemb ...... stallin but not with vimentin.
@nl
type
label
In vitro studies on the assemb ...... stallin but not with vimentin.
@ast
In vitro studies on the assemb ...... stallin but not with vimentin.
@en
In vitro studies on the assemb ...... stallin but not with vimentin.
@nl
prefLabel
In vitro studies on the assemb ...... stallin but not with vimentin.
@ast
In vitro studies on the assemb ...... stallin but not with vimentin.
@en
In vitro studies on the assemb ...... stallin but not with vimentin.
@nl
P2093
P1476
In vitro studies on the assemb ...... stallin but not with vimentin.
@en
P2093
Hutcheson AM
Quinlan RA
P304
P356
10.1016/S0014-4835(95)80009-3
P577
1995-02-01T00:00:00Z