(Q68158341)

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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Europe PubMed Central

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

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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Europe PubMed Central

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

22 September 2019

cross-linking reagent

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14 October 2022

1 reference

10.1111/J.1432-1033.1992.TB16992.X

https://api.crossref.org/works/10.1111/J.1432-1033.1992.TB16992.X

14 October 2022

author name string

N. Geisler

1

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14 October 2022

J. Schünemann

2

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14 October 2022

K. Weber

3

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14 October 2022

language of work or name

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National Center for Biotechnology Information

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14 October 2022

publication date

1 June 1992

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22 September 2019

15 June 1992

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National Center for Biotechnology Information

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=1606966

14 October 2022

full work available at URL

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

1 reference

10.1111/J.1432-1033.1992.TB16992.X

https://api.crossref.org/works/10.1111/J.1432-1033.1992.TB16992.X

14 October 2022

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

1 reference

10.1111/J.1432-1033.1992.TB16992.X

https://api.crossref.org/works/10.1111/J.1432-1033.1992.TB16992.X

14 October 2022

1 reference

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22 September 2019

206

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22 September 2019

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22 September 2019

841-852

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22 September 2019

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

1

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10.1111/J.1432-1033.1992.TB16992.X

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The fibrillar substructure of keratin filaments unraveled.

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Alterations in the phenotype of plant cells studied by NH(2)-terminal amino acid-sequence analysis of proteins electroblotted from two-dimensional gel-separated total extracts.

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Chemical studies on methionyl-tRNA synthetase from Escherichia coli

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Elucidating the early stages of keratin filament assembly

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

8

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The structure of the alpha-keratin microfibril

9

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Intermediate filaments in alpha-keratins

11

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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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Isolation of polymerization‐competent vimentin from porcine eye lens tissue

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

16

1 reference

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

17

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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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14 October 2022

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

21

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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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Molecular architecture of the neurofilament. II. Reassembly process of neurofilament L protein in vitro

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Modulation of desmin intermediate filament assembly by a monoclonal antibody

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Assembly of vimentin in vitro and its implications concerning the structure of intermediate filaments

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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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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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

31

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

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Heterotypic tetramer (A2D2) complexes of non-epidermal keratins isolated from cytoskeletons of rat hepatocytes and hepatoma cells

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Characterization of dimer subunits of intermediate filament proteins.

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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

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Identification of a distinct soluble subunit of an intermediate filament protein: tetrameric vimentin from living cells

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N-hydroxysulfosuccinimide active esters: bis(N-hydroxysulfosuccinimide) esters of two dicarboxylic acids are hydrophilic, membrane-impermeant, protein cross-linkers

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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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Analysis of the mechanism of assembly of mouse keratin 1/keratin 10 intermediate filaments in vitro suggests that intermediate filaments are built from multiple oligomeric units rather than a unique tetrameric building block

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Molecular interactions in paracrystals of a fragment corresponding to the alpha-helical coiled-coil rod portion of glial fibrillary acidic protein: evidence for an antiparallel packing of molecules and polymorphism related to intermediate filament s

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

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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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