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Nexilin: a novel actin filament-binding protein localized at cell-matrix adherens junction
scientific journal article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
9832551
retrieved
31 January 2017
title
Nexilin: a novel actin filament-binding protein localized at cell-matrix adherens junction
(English)
1 reference
stated in
PubMed
PubMed ID
9832551
retrieved
31 January 2017
main subject
actin filament
1 reference
based on heuristic
inferred from title
author name string
T. Ohtsuka
series ordinal
1
1 reference
stated in
PubMed
PubMed ID
9832551
retrieved
31 January 2017
H. Nakanishi
series ordinal
2
1 reference
stated in
PubMed
PubMed ID
9832551
retrieved
31 January 2017
W. Ikeda
series ordinal
3
1 reference
stated in
PubMed
PubMed ID
9832551
retrieved
31 January 2017
A. Satoh
series ordinal
4
1 reference
stated in
PubMed
PubMed ID
9832551
retrieved
31 January 2017
Y. Momose
series ordinal
5
1 reference
stated in
PubMed
PubMed ID
9832551
retrieved
31 January 2017
H. Nishioka
series ordinal
6
1 reference
stated in
PubMed
PubMed ID
9832551
retrieved
31 January 2017
Y. Takai
series ordinal
7
1 reference
stated in
PubMed
PubMed ID
9832551
retrieved
31 January 2017
language of work or name
English
0 references
publication date
30 November 1998
1 reference
stated in
PubMed
PubMed ID
9832551
retrieved
31 January 2017
published in
Journal of Cell Biology
1 reference
stated in
PubMed
PubMed ID
9832551
retrieved
31 January 2017
volume
143
1 reference
stated in
PubMed
PubMed ID
9832551
retrieved
31 January 2017
page(s)
1227–1238
1 reference
stated in
PubMed
PubMed ID
9832551
retrieved
31 January 2017
issue
5
1 reference
stated in
PubMed
PubMed ID
9832551
retrieved
31 January 2017
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Molecular cloning of chick cardiac muscle tensin. Full-length cDNA sequence, expression, and characterization.
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Unphosphorylated gelsolin is localized in regions of cell-substratum contact or attachment in Rous sarcoma virus-transformed rat cells
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Crossref
reference URL
https://api.crossref.org/works/10.1083%2FJCB.143.5.1227
retrieved
21 January 2018
Purification of muscle actin
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9832551
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Actin-binding proteins
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9832551
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Molecular properties and functions in vitro of chicken smooth-muscle alpha-actinin in comparison with those of striated-muscle alpha-actinins
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9832551
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Direct binding of F-actin to ponticulin, an integral plasma membrane glycoprotein
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9832551
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Purification and characterization of zyxin, an 82,000-dalton component of adherens junctions
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9832551
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identification and subcellular location of talin in various cell types and tissues by means of [125I]vinculin overlay, immunoblotting and immunocytochemistry
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9832551
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Adhesions of fibroblasts to substratum during contact inhibition observed by interference reflection microscopy
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9832551
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1083/JCB.143.5.1227
0 references
PMCID
2133087
0 references
PubMed ID
9832551
1 reference
stated in
PubMed
PubMed ID
9832551
retrieved
31 January 2017
ResearchGate publication ID
277377968
0 references
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