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Type 3 and type 1 ryanodine receptors are localized in triads of the same mammalian skeletal muscle fibers
scientific journal article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
10444070
retrieved
31 January 2017
title
Type 3 and type 1 ryanodine receptors are localized in triads of the same mammalian skeletal muscle fibers
(English)
1 reference
stated in
PubMed
PubMed ID
10444070
retrieved
31 January 2017
main subject
Ryanodine receptor 3
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stated in
GOA release 2020-03-11
Calcium channel, voltage-dependent, L type, alpha 1S subunit
1 reference
stated in
GOA release 2020-03-11
Ryanodine receptor 1, skeletal muscle
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GOA release 2020-03-11
author name string
B. E. Flucher
series ordinal
1
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stated in
PubMed
PubMed ID
10444070
retrieved
31 January 2017
A. Conti
series ordinal
2
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stated in
PubMed
PubMed ID
10444070
retrieved
31 January 2017
H. Takeshima
series ordinal
3
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stated in
PubMed
PubMed ID
10444070
retrieved
31 January 2017
V. Sorrentino
series ordinal
4
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stated in
PubMed
PubMed ID
10444070
retrieved
31 January 2017
language of work or name
English
0 references
publication date
9 August 1999
1 reference
stated in
PubMed
PubMed ID
10444070
retrieved
31 January 2017
published in
Journal of Cell Biology
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stated in
PubMed
PubMed ID
10444070
retrieved
31 January 2017
volume
146
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stated in
PubMed
PubMed ID
10444070
retrieved
31 January 2017
issue
3
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stated in
PubMed
PubMed ID
10444070
retrieved
31 January 2017
page(s)
621–630
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stated in
PubMed
PubMed ID
10444070
retrieved
31 January 2017
cites work
Requirement for the ryanodine receptor type 3 for efficient contraction in neonatal skeletal muscles
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PubMed Central
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Ca(2+)-induced Ca2+ release in myocytes from dyspedic mice lacking the type-1 ryanodine receptor
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Excitation-contraction uncoupling and muscular degeneration in mice lacking functional skeletal muscle ryanodine-receptor gene
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PubMed Central
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Molecular cloning of cDNA encoding the Ca2+ release channel (ryanodine receptor) of rabbit cardiac muscle sarcoplasmic reticulum
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17 March 2017
Molecular cloning of cDNA encoding human and rabbit forms of the Ca2+ release channel (ryanodine receptor) of skeletal muscle sarcoplasmic reticulum
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PubMed Central
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Expression of the ryanodine receptor type 3 in skeletal muscle. A new partner in excitation-contraction coupling?
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PubMed Central
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Local control model of excitation-contraction coupling in skeletal muscle
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PubMed Central
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29 September 2017
Functional characterization of the recombinant type 3 Ca2+ release channel (ryanodine receptor) expressed in HEK293 cells
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PubMed Central
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29 September 2017
Ryanodine receptors of striated muscles: a complex channel capable of multiple interactions
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PubMed Central
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29 September 2017
Coordinated incorporation of skeletal muscle dihydropyridine receptors and ryanodine receptors in peripheral couplings of BC3H1 cells
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PubMed Central
reference URL
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29 September 2017
Subtype specificity of the ryanodine receptor for Ca2+ signal amplification in excitation-contraction coupling
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PubMed Central
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29 September 2017
Ryanodine receptor Ca2+ release channels: does diversity in form equal diversity in function?
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PubMed Central
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29 September 2017
Formation of junctions involved in excitation-contraction coupling in skeletal and cardiac muscle.
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29 September 2017
Formation of triads without the dihydropyridine receptor alpha subunits in cell lines from dysgenic skeletal muscle
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PubMed Central
reference URL
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29 September 2017
Alpha and beta isoforms of ryanodine receptor from chicken skeletal muscle are the homologues of mammalian RyR1 and RyR3.
1 reference
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PubMed Central
reference URL
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29 September 2017
The Ca2+-release channel/ryanodine receptor is localized in junctional and corbular sarcoplasmic reticulum in cardiac muscle.
1 reference
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PubMed Central
reference URL
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29 September 2017
The fastest contracting muscles of nonmammalian vertebrates express only one isoform of the ryanodine receptor
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PubMed Central
reference URL
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29 September 2017
Triad formation: organization and function of the sarcoplasmic reticulum calcium release channel and triadin in normal and dysgenic muscle in vitro.
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PubMed Central
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29 September 2017
Primary structure and distribution of ryanodine-binding protein isoforms of the bullfrog skeletal muscle.
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PubMed Central
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29 September 2017
Molecular organization of transverse tubule/sarcoplasmic reticulum junctions during development of excitation-contraction coupling in skeletal muscle
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2150550
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29 September 2017
The role of Ca2+ ions in excitation-contraction coupling of skeletal muscle fibres
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PubMed Central
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29 September 2017
Immunolocalization of sarcolemmal dihydropyridine receptor and sarcoplasmic reticular triadin and ryanodine receptor in rabbit ventricle and atrium
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PubMed Central
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29 September 2017
Abnormal junctions between surface membrane and sarcoplasmic reticulum in skeletal muscle with a mutation targeted to the ryanodine receptor
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2150550
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29 September 2017
Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle
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PubMed Central
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29 September 2017
Molecular cloning and characterization of the ryanodine receptor/junctional channel complex cDNA from skeletal muscle sarcoplasmic reticulum
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PubMed Central
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29 September 2017
Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor.
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PubMed Central
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29 September 2017
Foot protein isoforms are expressed at different times during embryonic chick skeletal muscle development
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PubMed Central
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29 September 2017
Charge movement and the nature of signal transduction in skeletal muscle excitation-contraction coupling
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PubMed Central
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29 September 2017
Functional properties of the ryanodine receptor type 3 (RyR3) Ca2+ release channel
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PubMed Central
reference URL
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3 June 2018
Dyspedic mouse skeletal muscle expresses major elements of the triadic junction but lacks detectable ryanodine receptor protein and function
1 reference
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PubMed Central
reference URL
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3 June 2018
Differential distribution of ryanodine receptor type 3 (RyR3) gene product in mammalian skeletal muscles
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2150550
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3 June 2018
Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor.
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2150550
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3 June 2018
The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2150550
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3 June 2018
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PubMed Central
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3 June 2018
Primary structure and functional expression from cDNA of the cardiac ryanodine receptor/calcium release channel.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2150550
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3 June 2018
Expression of a ryanodine receptor-Ca2+ channel that is regulated by TGF-beta
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2150550
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3 June 2018
Purification and characterization of ryanodine receptor 3 from mammalian tissue.
1 reference
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PubMed Central
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27 November 2018
Contractile impairment and structural alterations of skeletal muscles from knockout mice lacking type 1 and type 3 ryanodine receptors.
1 reference
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PubMed Central
reference URL
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27 November 2018
Generation and characterization of mutant mice lacking ryanodine receptor type 3.
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PubMed Central
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27 November 2018
Monoclonal antibody identifies a 200-kDa subunit of the dihydropyridine-sensitive calcium channel
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10444070
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Embryonic chicken skeletal muscle cells fail to develop normal excitation-contraction coupling in the absence of the alpha ryanodine receptor. Implications for a two-ryanodine receptor system
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10444070
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Absence of Ca2+ current facilitation in skeletal muscle of transgenic mice lacking the type 1 ryanodine receptor
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10444070
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Expression of the ryanodine receptor type 3 calcium release channel during development and differentiation of mammalian skeletal muscle cells
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10444070
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Characterization of type 3 ryanodine receptor (RyR3) of sarcoplasmic reticulum from rabbit skeletal muscles
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10444070
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
A monoclonal antibody to the Ca2+-ATPase of cardiac sarcoplasmic reticulum cross-reacts with slow type I but not with fast type II canine skeletal muscle fibers: an immunocytochemical and immunochemical study
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10444070
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1083/JCB.146.3.621
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1326338
OpenCitations bibliographic resource ID
1326338
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1326338
PMCID
2150550
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1326338
PubMed ID
10444070
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1326338
ResearchGate publication ID
12855888
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