Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation. - Wikidata - wikimedia - TriplyDB

Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation.

Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation.

http://www.wikidata.org/entity/Q34190203

about

Abnormal calcium cycling and cardiac arrhythmias associated with the human Ser96Ala genetic variant of histidine-rich calcium-binding protein Review of RyR1 pathway and associated pathomechanisms Calsequestrin 2 (CASQ2) mutations increase expression of calreticulin and ryanodine receptors, causing catecholaminergic polymorphic ventricular tachycardia Anesthetic- and heat-induced sudden death in calsequestrin-1-knockout mice Calsequestrin content and SERCA determine normal and maximal Ca2+ storage levels in sarcoplasmic reticulum of fast- and slow-twitch fibres of rat Reorganized stores and impaired calcium handling in skeletal muscle of mice lacking calsequestrin-1 Store-dependent deactivation: cooling the chain-reaction of myocardial calcium signaling.Modulation of cardiac ryanodine receptor channels by alkaline earth cations A skeletal muscle ryanodine receptor interaction domain in triadin Couplons in rat atria form distinct subgroups defined by their molecular partners.The conformation of calsequestrin determines its ability to regulate skeletal ryanodine receptors.Calcium and arrhythmogenesis.On the footsteps of Triadin and its role in skeletal muscle C-terminal residues of skeletal muscle calsequestrin are essential for calcium binding and for skeletal ryanodine receptor inhibition Retrograde regulation of STIM1-Orai1 interaction and store-operated Ca2+ entry by calsequestrin.The changes in Ca2+ sparks associated with measured modifications of intra-store Ca2+ concentration in skeletal muscle.Triadin binding to the C-terminal luminal loop of the ryanodine receptor is important for skeletal muscle excitation contraction coupling.Luminal Ca2+ regulation of single cardiac ryanodine receptors: insights provided by calsequestrin and its mutants Calcium-dependent inactivation terminates calcium release in skeletal muscle of amphibians.Tricyclic antidepressant amitriptyline alters sarcoplasmic reticulum calcium handling in ventricular myocytes Mechanism of calsequestrin regulation of single cardiac ryanodine receptor in normal and pathological conditions.Ryanodine receptor-mediated arrhythmias and sudden cardiac death.Facilitated maturation of Ca2+ handling properties of human embryonic stem cell-derived cardiomyocytes by calsequestrin expression.Neuronal Na+ Channels Are Integral Components of Pro-arrhythmic Na+/Ca2+ Signaling Nanodomain That Promotes Cardiac Arrhythmias During β-adrenergic Stimulation.Trifluoperazine: a rynodine receptor agonist.Ryanodine receptor luminal Ca2+ regulation: swapping calsequestrin and channel isoforms.Junctin and triadin each activate skeletal ryanodine receptors but junctin alone mediates functional interactions with calsequestrin.Functional interaction between calsequestrin and ryanodine receptor in the heart.Characterization of Ca(2+)-Dependent Protein-Protein Interactions within the Ca(2+) Release Units of Cardiac Sarcoplasmic Reticulum.Organization of junctional sarcoplasmic reticulum proteins in skeletal muscle fibers.Core skeletal muscle ryanodine receptor calcium release complex.When sparks get old.Knocking down type 2 but not type 1 calsequestrin reduces calcium sequestration and release in C2C12 skeletal muscle myotubes.A possible role of the junctional face protein JP-45 in modulating Ca2+ release in skeletal muscle.Inhibition of SERCA pumps induces desynchronized RyR activation in overloaded internal Ca2+ stores in smooth muscle cells.The role of luminal Ca regulation in Ca signaling refractoriness and cardiac arrhythmogenesis.Growth hormone secretagogues prevent dysregulation of skeletal muscle calcium homeostasis in a rat model of cisplatin-induced cachexia.Role of calsequestrin evaluated from changes in free and total calcium concentrations in the sarcoplasmic reticulum of frog cut skeletal muscle fibres.Ryanodine Receptor Open Times Are Determined in the Closed State

P2860

Q24338370-27713242-0646-4271-A16A-CB7A4858A3C4 Q28078420-310D4161-668F-4512-9D47-7D87E6D0934C Q28235110-231AB560-45D8-4CBA-AD96-D7E7C575CDD2 Q28511309-1EEF30AA-3900-4695-8219-F7FEE3CC9682 Q28572127-038C84AD-2294-4F20-A92A-E187D1EC2F91 Q28589478-A41A05FE-6C84-4A11-9A20-DCCC80C87088 Q33798663-454078DB-FA99-4F06-8482-667254AD98A8 Q34062579-B062586E-465F-4730-9B60-8FEAC8021A86 Q34399431-8AE56F54-46A5-45BD-9748-00DDF4189879 Q34667639-7C5F8806-490C-4CE5-8AC2-BAB37C00D13E Q34829628-7BEEFCDB-51B9-430D-B14D-66C376DC6025 Q35095089-9A900318-CFD0-4620-AF89-CB81B24BD692 Q35193342-8A62B120-157C-435C-9FA4-2F5B3AD080D0 Q35312872-8ABE0017-ACF8-4D20-828B-21DCDF65D59F Q35754576-9535E0F5-6024-42CB-8C7B-56B134905E5A Q36295762-2DBF040C-3F95-4776-8C26-BB4308A94059 Q36296083-A04C65A1-1F0E-488A-A351-FCAC16BBB236 Q36517742-5384A2B3-7243-47DB-A99E-0B0584387F11 Q36517766-26718504-B60F-4F9A-A9DA-0B0EC3FEE2DB Q37038915-F027964A-30CE-4A6E-936C-244E091A07AE Q37055484-476DF451-E258-4506-8FA5-95A1DB3F275E Q37248371-946BB268-18E2-4BCE-9820-2E4090057098 Q37264115-C854CB88-E692-4EE0-BF71-CC906F3E21DF Q37341328-3938DF86-4180-4B81-BFD6-7C1C2D15A08D Q37365077-3D790B27-1F61-445D-858C-181F6F6C3329 Q37373399-CDCB1D05-285B-4BE5-982B-C042580B946B Q37422708-975949B1-947A-4925-80AA-ABF2CFD447E6 Q38056435-3C06FF1C-0FC5-4EF9-829A-B28214759D0D Q38541159-C2480A60-D01D-4D3D-939B-CEB3DE0E4556 Q38587629-E88A4409-4B5C-4642-961C-FAD57597EADB Q38970694-3184DF0B-45CA-4278-A545-CFE4477D730B Q39740498-9FA3CDD5-AD3E-4AF4-9406-9BBC2703CA1D Q40295793-BCF50AA7-1687-4423-A2FF-9A0A76895D8F Q40327584-A1D56521-7CB8-4438-857E-7B6593EABCAE Q43182559-CE90D500-A99B-4592-8D39-EA28B35165A1 Q48256510-0FBB7483-FE2E-4D33-A7EF-2F3805C5C677 Q50201348-019CDC64-224F-495D-90BA-6E3CF2A1913C Q50703602-701FBA36-9DE8-4E0B-A4E9-358CA2B24502 Q57044287-414394B4-C9F6-4B3F-9554-CE3FE7E57A4B

P2860

Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation.

http://www.wikidata.org/entity/Q34190203

description

2005 nî lūn-bûn

@nan

2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Regulation of ryanodine recept ...... inal Ca2+ and phosphorylation.

@ast

Regulation of ryanodine recept ...... inal Ca2+ and phosphorylation.

@en

Regulation of ryanodine recept ...... inal Ca2+ and phosphorylation.

@nl

type

label

Regulation of ryanodine recept ...... inal Ca2+ and phosphorylation.

@ast

Regulation of ryanodine recept ...... inal Ca2+ and phosphorylation.

@en

Regulation of ryanodine recept ...... inal Ca2+ and phosphorylation.

@nl

prefLabel

Regulation of ryanodine recept ...... inal Ca2+ and phosphorylation.

@ast

Regulation of ryanodine recept ...... inal Ca2+ and phosphorylation.

@en

Regulation of ryanodine recept ...... inal Ca2+ and phosphorylation.

@nl

P1433

Q34190203-B345856B-4D0E-4302-B73E-4967C7F4FF02

P1476

Q34190203-AD323F77-BBF0-4684-B34D-37FA06243883

P2093

Q34190203-2243C0DB-728E-49C9-BBA3-6F217A2BD0B7

Q34190203-3ED326E5-26C6-453A-99CB-B539F6436273

Q34190203-AF922272-A193-48EC-A49F-15190CD76983

Q34190203-BABF5A95-4BE8-450A-A1FD-1DBD46854927

Q34190203-D6CD62E5-EC82-47FA-AECE-364E7E99E27C

P2860

Q34190203-060A6764-575E-4084-BDE0-87B62061AE46

Q34190203-0CF0CA8E-E186-4716-BA0C-5E9C1E0153B7

Q34190203-1E37D482-B521-4F55-8DA8-27D1A60055F4

Q34190203-2B1FEB77-BE30-443B-85E8-BE170D883302

Q34190203-2D3AFED1-AD77-4245-AD3F-D8D347E64622

Q34190203-374CF835-DFF7-4D19-8466-06FC2EE30802

Q34190203-40FB319F-F182-433D-952C-E0545C1A66B4

Q34190203-42CC795F-1EB0-44B5-A28B-026718DEE5EE

Q34190203-43D2FFC9-5C9A-450B-9E39-DAEE01CC5B2C

Q34190203-45E4E319-B70C-4C1F-AEF5-C66A92E0FCF2

P304

Q34190203-129901DF-6CBE-4A6C-AEEF-83E88AD7E358

P31

Q34190203-1C792D5F-2C2E-4C11-9117-E1BDA84F2F85

P356

Q34190203-8FC2DF85-FD05-4CE6-B09F-07C91866A169

P407

Q34190203-7455A05C-A402-4D25-BE8A-02FFF0523554

P433

Q34190203-66BE47E1-94B5-4594-890A-1493BBCB4DC3

P478

Q34190203-DA68C5F8-E680-41EE-9DD6-05AF77FD58A7

P50

Q34190203-7D316BBA-D943-4C66-8106-7BD6EFC93F17

P577

Q34190203-12D8FCE2-F0A3-4546-84E9-0409E34450C4

P5875

Q34190203-DC4793C5-77A4-4834-B664-5140D2089784

P698

Q34190203-0112E36A-5181-412B-A93C-FF3A686973AA

P921

Q34190203-A233D55E-642B-47AC-AA7B-0AF9FEFC075B

P932

Q34190203-E41A5887-36A0-41B0-81C6-ADFB39364CFE

P356

BIOPHYSJ.104.051441

P1433

Biophysical Journal

P1476

Regulation of ryanodine recept ...... minal Ca2+ and phosphorylation

@en

P2093

Derek R Laver

http://www.w3.org/2001/XMLSchema#string

Lan Wei

http://www.w3.org/2001/XMLSchema#string

Magdolna Varsányi

http://www.w3.org/2001/XMLSchema#string

Marco G Casarotto

http://www.w3.org/2001/XMLSchema#string

Nicole A Beard

http://www.w3.org/2001/XMLSchema#string

P2860

The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium.

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum

Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane

Phosphorylation of cardiac and skeletal muscle calsequestrin isoforms by casein kinase II. Demonstration of a cluster of unique rapidly phosphorylated sites in cardiac calsequestrin

Different Ca2+ releasing action of caffeine and depolarisation in skeletal muscle fibres of the rat

Calsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channels

Characterization of the binding and phosphorylation of cardiac calsequestrin by epsilon protein kinase C

Polymerization of calsequestrin. Implications for Ca2+ regulation.

Functional interaction of the cytoplasmic domain of triadin with the skeletal ryanodine receptor.

P304

3444-3454

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1529/BIOPHYSJ.104.051441

http://www.w3.org/2001/XMLSchema#string

P407

P433

5

http://www.w3.org/2001/XMLSchema#string

P478

88

http://www.w3.org/2001/XMLSchema#string

P50

Angela F Dulhunty

P577

2005-02-24T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

8003020

http://www.w3.org/2001/XMLSchema#string

P698

15731387

http://www.w3.org/2001/XMLSchema#string

P921

phosphorylation

P932

1305491

http://www.w3.org/2001/XMLSchema#string