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The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins.

Data up to Jan 2025

Published1982
Citations432
References36

Total Citations Per Year

Abstract

References (36)

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Proteinchemical characterization of three structurally distinct domains along the protofilament unit of desmin 10 nm filaments

1982 • 242 citations

Intermediate Filaments

1982 • 236 citations

Lac Repressor

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1977 • 169 citations

Heteropolymer filaments of vimentin and desmin in vascular smooth muscle tissue and cultured baby hamster kidney cells demonstrated by chemical crosslinking.

1982 • 157 citations

Comparison of the proteins of two immunologically distinct intermediate-sized filaments by amino acid sequence analysis: desmin and vimentin.

1981 • 156 citations

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1981 • 146 citations

Intermediate filaments of baby hamster kidney (BHK-21) cells and bovine epidermal keratinocytes have similar ultrastructures and subunit domain structures.

1980 • 136 citations

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1976 • 131 citations

A periodic ultrastructure in intermediate filaments

1982 • 126 citations

Structure of the three-chain unit of the bovine epidermal keratin filament

1978 • 124 citations

Related amino acid sequences in neurofilaments and non-neuronal intermediate filaments

1982 • 122 citations

Intermediate-size Filaments: Changes in Synthesis and Distribution in Cells of the Myogenic and Neurogenic Lineages

1982 • 111 citations

Visualization of a 21-nm axial periodicity in shadowed keratin filaments and neurofilaments.

1982 • 100 citations

Structure of fibroblastic intermediate filaments: analysis of scanning transmission electron microscopy.

1982 • 85 citations

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1973 • 84 citations

Coiled coil formation and sequence regularities in the helical regions of α-keratin

1978 • 79 citations

Ten-nanometer filaments of hamster BHK-21 cells and epidermal keratin filaments have similar structures.

1978 • 72 citations

Suberimidate crosslinking shows that a rod‐shaped, low cystine, high helix protein prepared by limited proteolysis of reduced wool has four protein chains

1978 • 71 citations

Amino acid sequences of α-helical segments from S-carboxymethylkerateine-A. Complete sequence of a type-II segment

1978 • 66 citations

Heterogeneity of Intermediate Filaments Assembled In Vitro

1982 • 61 citations

Studies on microfibrils from α-keratin

1976 • 49 citations

The structural relation between intermediate filament proteins in living cells and the alpha-keratins of sheep wool.

1982 • 49 citations

Structural Studies on the Microfibrillar Proteins of Wool: Characterization of the a-Helix-Rich Particle Produced by Chymotryptic Digestion

1981 • 38 citations

Antibodies against merokeratin from sheep wool decorate cytokeratin filaments in non-keratinizing epithelial cells.

1980 • 29 citations

Isolation and characterization of a soluble, immunoactive peptide of glial fibrillary acidic protein

1981 • 19 citations

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The amino acid sequence of chicken muscle desmin provides a common structural model for… (1982) – The EMBO Journal | Metascience Observatory Explorer