In vitro studies on the assembly properties of the lens proteins CP49, CP115: Coassembly with α-crystallin but not with vimentin
- 1 February 1995
- journal article
- Published by Elsevier in Experimental Eye Research
- Vol. 60 (2) , 181-192
- https://doi.org/10.1016/s0014-4835(95)80009-3
Abstract
No abstract availableKeywords
This publication has 54 references indexed in Scilit:
- The 47-kD lens-specific protein phakinin is a tailless intermediate filament protein and an assembly partner of filensin.The Journal of cell biology, 1993
- Bovine filensin possesses primary and secondary structure similarity to intermediate filament proteins.The Journal of cell biology, 1993
- Keratin Intermediate Filament StructureJournal of Molecular Biology, 1993
- cDNA sequence analysis of CP94: Rat lens fiber cell beaded-filament structural protein shows homology to cytokeratinsBiochemical and Biophysical Research Communications, 1992
- The 53kDa polypeptide component of the bovine fibre cell cytoskeleton is derived from the 115kDa beaded filament protein: evidence for a fibre cell specific intermediate filament proteinCurrent Eye Research, 1992
- Reconstitution of the filamentous backbone of lens beaded-chain filaments from a purified 49kD polypeptideCurrent Eye Research, 1991
- Expression of NF-L and NF-M in fibroblasts reveals coassembly of neurofilament and vimentin subunits.The Journal of cell biology, 1989
- Heterotypic tetramer (A2D2) complexes of non-epidermal keratins isolated from cytoskeletons of rat hepatocytes and hepatoma cellsJournal of Molecular Biology, 1984
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970