The second Ca2+-binding domain of the Na+ Ca2+ exchanger is essential for regulation: crystal structures and mutational analysis. - Test2 - elhamkhani - TriplyDB

The second Ca2+-binding domain of the Na+ Ca2+ exchanger is essential for regulation: crystal structures and mutational analysis.

The second Ca2+-binding domain of the Na+ Ca2+ exchanger is essential for regulation: crystal structures and mutational analysis.

http://www.wikidata.org/entity/Q27648908

about

Na⁺ transport in the normal and failing heart - remember the balance Structural Features of Ion Transport and Allosteric Regulation in Sodium-Calcium Exchanger (NCX) Proteins Ca2+ regulation of ion transport in the Na+/Ca2+ exchanger Structure and Functional Analysis of a Ca2+ Sensor Mutant of the Na+/Ca2+ Exchanger Ca2+ regulation in the Na+/Ca2+ exchanger features a dual electrostatic switch mechanism Structural basis for autoregulation of the zinc transporter YiiP Structural Basis of the Ca2+ Inhibitory Mechanism of Drosophila Na+/Ca2+ Exchanger CALX and Its Modification by Alternative Splicing NMR structure note: solution structure of Ca²⁺ binding domain 2B of the third isoform of the Na⁺/Ca²⁺ exchanger Na+/Ca2+ exchange and Na+/K+-ATPase in the heart The Na-K-ATPase and Calcium-Signaling Microdomains Crystal structures of progressive Ca2+ binding states of the Ca2+ sensor Ca2+ binding domain 1 (CBD1) from the CALX Na+/Ca2+ exchanger reveal incremental conformational transitions.Structure-based dynamic arrays in regulatory domains of sodium-calcium exchanger (NCX) isoforms.Activation of the cardiac Na(+)-Ca(2+) exchanger by sorcin via the interaction of the respective Ca(2+)-binding domains.A common Ca2+-driven interdomain module governs eukaryotic NCX regulation Transmembrane segment packing of the Na(+)/Ca(2+) exchanger investigated with chemical cross-linkers Ca2+-dependent structural rearrangements within Na+-Ca2+ exchanger dimers.Ca2+ binding alters the interdomain flexibility between the two cytoplasmic calcium-binding domains in the Na+/Ca2+ exchanger Proton-sensing Ca2+ binding domains regulate the cardiac Na+/Ca2+ exchanger.Calmodulin Interacts with the Sodium/Calcium Exchanger NCX1 to Regulate Activity.Getting a grip on calcium regulation.Direct Loading of the purified endogenous inhibitor into the cytoplasm of patched cardiomyocytes blocks the ion currents and calcium transport through the NCX1 protein.Structural arrangement of the intracellular Ca2+ binding domains of the cardiac Na+/Ca2+ exchanger (NCX1.1): effects of Ca2+ binding.Indirect role of Ca2+ in the assembly of extracellular matrix proteins Conformational changes of a Ca2+-binding domain of the Na+/Ca2+ exchanger monitored by FRET in transgenic zebrafish heart.Na+ transport in cardiac myocytes; Implications for excitation-contraction coupling.beta-adrenergic regulation of a novel isoform of NCX: sequence and expression of shark heart NCX in human kidney cells Roles of two Ca2+-binding domains in regulation of the cardiac Na+-Ca2+ exchanger.Structural and dynamic aspects of Ca2+ and Mg2+ binding of the regulatory domains of the Na+/Ca2+ exchanger.20 years from NCX purification and cloning: milestones.Function and regulation of the Na+-Ca2+ exchanger NCX3 splice variants in brain and skeletal muscle.Interactions between calcium intake and polymorphisms in genes essential for calcium reabsorption and risk of colorectal neoplasia in a two-phase study.How a helix imposes palmitoylation of a membrane protein: What one can learn from NCX.Crystallization and preliminary X-ray crystallographic analysis of Ca2+-free primary Ca2+-sensor of Na+/Ca2+ exchanger.Modeling Na+-Ca2+ exchange in the heart: Allosteric activation, spatial localization, sparks and excitation-contraction coupling.Population shift underlies Ca2+-induced regulatory transitions in the sodium-calcium exchanger (NCX).Essential role of the CBD1-CBD2 linker in slow dissociation of Ca2+ from the regulatory two-domain tandem of NCX1.Structure-dynamic determinants governing a mode of regulatory response and propagation of allosteric signal in splice variants of Na+/Ca2+ exchange (NCX) proteins.Cardiac Na+-Ca2+ exchanger: dynamics of Ca2+-dependent activation and deactivation in intact myocytes.Characterization of zebrafish (Danio rerio) NCX4: a novel NCX with distinct electrophysiological properties.Molecular determinants of pH regulation in the cardiac Na+-Ca2+ exchanger.

P2860

Q24338863-7AF24DE9-10F6-4CC5-B65D-C4CFCBDAA483 Q26768150-E15288AE-1630-42B8-BA95-27C6829FFE3B Q26864939-7FC83EBF-77E3-4CA3-ADF4-C2A643C58996 Q27654518-CAEF18A4-4423-45F6-A23D-6FB4B7B27693 Q27656957-4B0C8F20-654B-4FE6-B10E-B446F501CE8F Q27657426-53A708BD-B043-4F1D-8FD2-7A6EEF9868F6 Q27675064-A2B85A15-7CA6-46DD-8E54-6AD417372111 Q27681769-F26F64DC-9884-4721-8AC8-AC5402F3A028 Q28258875-49D86A27-2AB7-4E59-8A06-AD9A7AFFE6DF Q29543366-E135EFB6-202A-4B78-9437-E3A7755E4BB6 Q33593960-9A0F5071-E882-4156-B707-AE958798B05F Q33681272-0CA0015F-FC5E-4671-91E1-F9B0AED58AD9 Q34218092-C91605F9-E03F-4ED7-AD77-4F3DE6CB621E Q34328498-B69B0940-0640-495B-8BB8-5D198D90CF4C Q34424523-581DB008-E357-4FD7-9EC0-5EC2D81708F9 Q34533736-6C84F840-DEAE-4CD0-A6CE-0B3480BC84C7 Q35213277-9610595B-F029-4967-B835-6396C693D6F1 Q35309453-1E4F0C90-8CEB-4B37-8363-18FD4C96A59E Q35793343-2A317287-69DE-453A-89C5-7232AA0CE29E Q36276750-6E440803-2175-48D1-942F-BC1C1E6770B1 Q36467498-6D9888BE-3AA2-42BE-BAD8-808ADB20ED2A Q36596273-1187F875-B624-4FFB-8779-9709B7DE15D1 Q36717691-7F494CDD-08D6-4AE7-BAC6-5AA1E702BAC3 Q36842324-6AB917FA-1545-4580-B7C5-527C83A866DA Q37159984-06C0D8D7-44F1-4753-9D58-BF35E2FDFDE2 Q37276162-AF7B4B50-BCB3-4152-A9F7-FBD91A59FD4B Q37432101-54E36B05-8B8E-4544-B6C3-3F4028218BC2 Q37995729-B0AD6BFC-FC2B-418B-91C8-0B071749E5EA Q38066036-4DAB6801-1DEE-4BD4-BB88-B7B06F173317 Q39997971-ACE5D701-4DD0-482A-8C7E-B162EB23D548 Q40185669-BFB519F9-CAB6-445A-B1DE-A7FD5A0B5B19 Q41063082-E29B96E2-03E4-4524-A89D-845F76B727CB Q41338627-13A4D6A0-511B-4880-B7DC-15A1233A940C Q41649726-3CDEE923-8A56-4DA8-BCC4-85FA8855477B Q41974945-6DBC61A8-4E25-44CC-80AF-48321BF2A785 Q42136151-8AB207BA-46B1-4BDA-ACFC-C9EADD5DE258 Q43696452-37688F76-9FDE-49BE-B2B8-348C8E747682 Q45639318-CEF141B4-0F05-490F-B4AA-47E560789FC9 Q46084878-F4283F50-5A45-4813-856C-AEA089FA7555 Q48307290-CED00491-172B-49F4-89F0-CBE3BA421A93

P2860

The second Ca2+-binding domain of the Na+ Ca2+ exchanger is essential for regulation: crystal structures and mutational analysis.

http://www.wikidata.org/entity/Q27648908

description

2007 nî lūn-bûn

@nan

2007 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

The second Ca2+-binding domain ...... ctures and mutational analysis

@nl

The second Ca2+-binding domain ...... tures and mutational analysis.

@ast

The second Ca2+-binding domain ...... tures and mutational analysis.

@en

type

label

The second Ca2+-binding domain ...... ctures and mutational analysis

@nl

The second Ca2+-binding domain ...... tures and mutational analysis.

@ast

The second Ca2+-binding domain ...... tures and mutational analysis.

@en

prefLabel

The second Ca2+-binding domain ...... ctures and mutational analysis

@nl

The second Ca2+-binding domain ...... tures and mutational analysis.

@ast

The second Ca2+-binding domain ...... tures and mutational analysis.

@en

P1433

Q27648908-1DD98304-5511-422F-9E8D-FC054EEA9F31

P1476

Q27648908-6AF2302F-6B31-4541-A7BE-8573EEDBABC1

P2093

Q27648908-0887C315-9045-4FF7-AF78-022C71898C3F

Q27648908-0D3C42D1-AEB6-40B2-ABC9-2764BF539F38

Q27648908-5E966320-2F98-491C-9B9F-A8F33D98022F

Q27648908-6ACB29DC-8D13-4CF0-AB0D-7122B4A71703

Q27648908-82D65ABC-3C04-4AA9-A8D1-F4D85B363BA7

Q27648908-8318A730-4F5D-4F93-9FA8-3A820A6C81F0

Q27648908-CF34991A-EAFD-4DEC-9C33-C01299E8F262

P2860

Q27648908-05F2373D-409A-4EA3-B6FE-89F0B8FCD66E

Q27648908-1068B90B-49CB-4AD1-B742-607151A89F62

Q27648908-24A40C84-5EF3-47E0-A524-2FE7D26040D9

Q27648908-2CD13EC2-B98E-4A10-9780-D1720512D123

Q27648908-338FB049-5D89-4B5E-B898-F50FAD2B206F

Q27648908-4571DF71-E627-4503-A6C8-5E5635882E5F

Q27648908-522F2DED-E7D6-4F03-A63D-1114E7E42083

Q27648908-54CE273F-71EE-4BB9-8083-8B36AA012291

Q27648908-58568781-CFAC-436D-8D64-96E178E48779

Q27648908-7030653D-AB4C-4410-8622-AB8E33441884

P304

Q27648908-3CD17707-1FBC-48FC-B2BD-2BB5AF286530

P31

Q27648908-39C54CA6-5015-4C8B-AF82-A20110213262

P356

Q27648908-4925E989-29E3-4540-9112-90350271482D

P407

Q27648908-D0CABAF9-0D08-441C-A5D0-705DCFFA2B19

P433

Q27648908-F4277567-E39D-4B52-82A8-7BA0337FC044

P478

Q27648908-7E2AC2F1-3B7D-4472-BC40-FA740AE0E979

P50

Q27648908-F041A96D-606C-469B-B44E-DC8DA98B992E

P577

Q27648908-CF5F6730-399F-4F2B-AD79-C5EE0002B99D

P5875

Q27648908-0F4E9EAD-D73E-4AEA-965C-B348C9FA031E

P698

Q27648908-6556848A-A6BA-49B2-8282-D41EEEB69758

P921

Q27648908-2B9B4179-5FAE-4AEF-B8CE-B136669CCC55

P932

Q27648908-84E1FB49-5B9F-44FF-8C39-15CCE5ACEE1A

P356

PNAS.0707417104

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

The second Ca2+-binding domain ...... tures and mutational analysis.

@en

P2093

Debora A Nicoll

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

Duilio Cascio

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

Gabriel Mercado Besserer

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

Jeff Abramson

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

Kenneth D Philipson

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

Michela Ottolia

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

Vincent Chaptal

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

P2860

Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation.

Calx, a Na-Ca exchanger gene of Drosophila melanogaster

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Coot: model-building tools for molecular graphics

Likelihood-enhanced fast translation functions

Refinement of macromolecular structures by the maximum-likelihood method

The crystal structure of the primary Ca2+ sensor of the Na+/Ca2+ exchanger reveals a novel Ca2+ binding motif

C2-domains, structure and function of a universal Ca2+-binding domain

Small revisions to predicted distances around metal sites in proteins

P304

18467-18472

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

P31

scholarly article

P356

10.1073/PNAS.0707417104

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

P407

P433

47

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

P478

104

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

P50

P577

2007-10-25T00:00:00Z

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

P5875

5884293

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

P698

17962412

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

P921

crystal structure

P932

2141800

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