The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca(2+) and interacts with triadin.
about
Interaction of HRC (histidine-rich Ca(2+)-binding protein) and triadin in the lumen of sarcoplasmic reticulumThe role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium.Junctin and the histidine-rich Ca2+ binding protein: potential roles in heart failure and arrhythmogenesisTriadin regulation of the ryanodine receptor complexCalsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channelsJunctin is a prominent regulator of contractility in cardiomyocytesA retrograde signal from calsequestrin for the regulation of store-operated Ca2+ entry in skeletal muscleInteraction of annexin A6 with alpha actinin in cardiomyocytesAsprich: A novel aspartic acid-rich protein family from the prismatic shell matrix of the bivalve Atrina rigida.Dysregulated sarcoplasmic reticulum calcium release: potential pharmacological target in cardiac disease.Comparative transcriptome analysis of stylar canal cells identifies novel candidate genes implicated in the self-incompatibility response of Citrus clementinaRegulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation.Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin.A skeletal muscle ryanodine receptor interaction domain in triadinThe conformation of calsequestrin determines its ability to regulate skeletal ryanodine receptors.Calcium and arrhythmogenesis.D4cpv-calsequestrin: a sensitive ratiometric biosensor accurately targeted to the calcium store of skeletal muscle.Measurement of RyR permeability reveals a role of calsequestrin in termination of SR Ca(2+) release in skeletal muscleC-terminal residues of skeletal muscle calsequestrin are essential for calcium binding and for skeletal ryanodine receptor inhibitionRole of molecular charge and hydrophilicity in regulating the kinetics of crystal growthRole for SUR2A ED domain in allosteric coupling within the K(ATP) channel complex.Modulation of SR Ca release by luminal Ca and calsequestrin in cardiac myocytes: effects of CASQ2 mutations linked to sudden cardiac death.Regulatory roles of junctin in sarcoplasmic reticulum calcium cycling and myocardial function.Partial downregulation of junctin enhances cardiac calcium cycling without eliciting ventricular arrhythmias in mice.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.Triadin deletion induces impaired skeletal muscle functionCalsequestrin depolymerizes when calcium is depleted in the sarcoplasmic reticulum of working muscle.Functional interaction between calsequestrin and ryanodine receptor in the heart.Molecular and functional analyses of aspolin, a fish-specific protein extremely rich in aspartic acid.Identification and characterization of a novel secretory granule calcium-binding protein from the early branching eukaryote Giardia lamblia.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.Calsequestrin interacts directly with the cardiac ryanodine receptor luminal domain.Knocking down type 2 but not type 1 calsequestrin reduces calcium sequestration and release in C2C12 skeletal muscle myotubes.Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers.Triadins are not triad-specific proteins: two new skeletal muscle triadins possibly involved in the architecture of sarcoplasmic reticulumHead-to-tail oligomerization of calsequestrin: a novel mechanism for heterogeneous distribution of endoplasmic reticulum luminal proteins.Role of the JP45-Calsequestrin Complex on Calcium Entry in Slow Twitch Skeletal Muscles.Emerging roles of protein disulfide isomerase in cancer.
P2860
Q24291561-4D970A8A-E42C-4EA2-A50D-96D68F945B3AQ24319842-E3057272-72F4-481D-A6F3-F1E9CA2EBEB7Q24320070-CCDA4B42-AAE9-4833-BFFF-A10E087E9582Q26801317-E6CAF099-3C33-43DE-AC21-99F31B23D399Q28366867-391E8A90-0569-4AE4-9CCC-D4928AA3FD9BQ28565063-18376D6D-8BDD-4513-9CE3-DE8E83C78AE3Q28586041-81722DE5-A1A0-413D-BCFF-367D653C36E0Q30498156-491039C4-F1FB-482A-8D79-A38152E3B0E6Q31144542-F0873616-2CF7-4124-9D38-57553DDB400CQ33559348-6C35B3A6-6DFE-4FD5-AA40-51075046AE3CQ34158557-00C909EE-FBF7-4F23-BA40-CD2B595D675AQ34190203-4AA3AD5C-3D7F-454E-B4E6-D8E89BB60620Q34279088-EABE531B-38DF-47AA-9BF9-D0BDF300041FQ34399431-921A7CE1-8047-4C82-BC26-15B417290A43Q34829628-3444C2E6-DF06-4E84-A393-BED1121A8F7FQ35095089-AC62B207-5D20-458A-8A58-0A7E7F81A193Q35145288-A340871E-85A3-41D1-B840-53A915B430EFQ35145292-2402D7ED-5E62-4639-B2FC-3DA5F7745192Q35312872-C7866353-F860-497D-B355-8DEC247CB584Q35539898-EA2FB96F-2324-4071-B82F-837429792DA2Q36471331-954083FB-DC1B-443D-8761-53A7633FF3C7Q36791253-A6736ADC-98D7-4E88-AD1A-411DFE247ABFQ36995841-05D5A952-4DFC-46A3-9FE6-2089C921EF9EQ37200241-19841B03-B884-4E2F-B634-0D9B87042675Q37373399-34220948-A4F8-4BA8-AAC7-2C523B945D6FQ37422708-7977BD24-D810-402C-8FF8-BBD585096A32Q37454303-69F64623-00A7-4DB7-B98E-11E4E4177D62Q37612539-B4B356FC-94F6-44BD-BC4B-8373D27FDF09Q38056435-6D920847-D736-45F8-9D79-D9A478AC996BQ38340502-4AB11952-46AD-4F59-AE3A-EA7FFA1CAF5BQ38362431-22F9C0D5-5C84-4C60-8DDC-C800C7BC9871Q38541159-FAFD1752-FB53-4FBD-AC53-60108521F55CQ38587629-A81A0FF7-83B7-4B0C-86E6-CDFECC923493Q38734361-F5E6BF9E-880B-418E-BA2B-ACC10248F28CQ40295793-69929387-89C5-4F75-A3E2-CE2A897AB57AQ40298386-EA48BFBE-791C-4DCF-BC9F-E6565B0C969CQ41975814-96A2B633-8D6E-470F-8030-BEB8C8F2B6D3Q42114931-2A808CCD-35B6-490B-ACAD-E183ED44AD26Q42117082-3000C28A-DE7B-40EB-B2B1-DBF249EEDE32Q42357758-2AC321F1-D5B2-4D48-BA59-8E970DE984F4
P2860
The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca(2+) and interacts with triadin.
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
The asp-rich region at the car ...... +) and interacts with triadin.
@ast
The asp-rich region at the car ...... +) and interacts with triadin.
@en
type
label
The asp-rich region at the car ...... +) and interacts with triadin.
@ast
The asp-rich region at the car ...... +) and interacts with triadin.
@en
prefLabel
The asp-rich region at the car ...... +) and interacts with triadin.
@ast
The asp-rich region at the car ...... +) and interacts with triadin.
@en
P2093
P2860
P1433
P1476
The asp-rich region at the car ...... +) and interacts with triadin.
@en
P2093
P2860
P304
P356
10.1016/S0014-5793(00)02246-8
P407
P577
2000-12-01T00:00:00Z