Chemical cross-linking indicates a staggered and antiparallel protofilament of desmin intermediate filaments and characterizes one higher-level complex between protofilaments (Q68158341)

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scientific article published on June 15, 1992

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English	Chemical cross-linking indicates a staggered and antiparallel protofilament of desmin intermediate filaments and characterizes one higher-level complex between protofilaments	scientific article published on June 15, 1992

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scholarly article

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22 September 2019

Chemical cross-linking indicates a staggered and antiparallel protofilament of desmin intermediate filaments and characterizes one higher-level complex between protofilaments (English)

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22 September 2019

cross-linking reagent

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14 October 2022

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10.1111/J.1432-1033.1992.TB16992.X

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14 October 2022

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N. Geisler

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14 October 2022

J. Schünemann

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14 October 2022

K. Weber

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publication date

1 June 1992

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22 September 2019

15 June 1992

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14 October 2022

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https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1992.tb16992.x

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10.1111/J.1432-1033.1992.TB16992.X

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14 October 2022

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1992.tb16992.x/fullpdf

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10.1111/J.1432-1033.1992.TB16992.X

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14 October 2022

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22 September 2019

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22 September 2019

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22 September 2019

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22 September 2019

A new cleavable reagent for cross-linking and reversible immobilization of proteins

1

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Deletions in epidermal keratins leading to alterations in filament organization in vivo and in intermediate filament assembly in vitro

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

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

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Antiparallel orientation of the two double-stranded coiled-coils in the tetrameric protofilament unit of intermediate filaments

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Are the terminal domains in intermediate filaments organized as octameric complexes? Reevaluation of a recent suggestion

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The coiled coil of in vitro assembled keratin filaments is a heterodimer of type I and II keratins: use of site-specific mutagenesis and recombinant protein expression

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A synthetic peptide representing the consensus sequence motif at the carboxy-terminal end of the rod domain inhibits intermediate filament assembly and disassembles preformed filaments

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Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis

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Molecular architecture of the neurofilament. I. Subunit arrangement of neurofilament L protein in the intermediate-sized filament

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Modulation of desmin intermediate filament assembly by a monoclonal antibody

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Subunit structure of desmin and vimentin protofilaments and how they assemble into intermediate filaments

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Intermediate filament forming ability of desmin derivatives lacking either the amino-terminal 67 or the carboxy-terminal 27 residues

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The coiled-coil molecules of intermediate filaments consist of two parallel chains in exact axial register

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The structure of intermediate filaments

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The two coiled coils in the isolated rod domain of the intermediate filament protein desmin are staggered. A hydrodynamic analysis of tetramers and dimers

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Characterization of dimer subunits of intermediate filament proteins

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Organization of coiled-coil molecules in native mouse keratin 1/keratin 10 intermediate filaments: Evidence for alternating rows of antiparallel in-register and antiparallel staggered molecules

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Identifiers

10.1111/J.1432-1033.1992.TB16992.X

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:1606966%20AND%20SRC:MED&resulttype=core&format=json

22 September 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:1606966%20AND%20SRC:MED&resulttype=core&format=json

22 September 2019

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