Molecular mechanism of the calcium-induced conformational change in the spectrin EF-hands. - Wikidata - awgldk - TriplyDB

Molecular mechanism of the calcium-induced conformational change in the spectrin EF-hands.

Molecular mechanism of the calcium-induced conformational change in the spectrin EF-hands.

http://www.wikidata.org/entity/Q40789626

about

Spectrin-based skeleton as an actor in cell signaling Structure and calcium-binding studies of calmodulin-like domain of human non-muscle α-actinin-1.The structure of the ankyrin-binding site of -spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties The carboxyterminal EF domain of erythroid alpha-spectrin is necessary for optimal spectrin-actin binding Analysis of novel sph (spherocytosis) alleles in mice reveals allele-specific loss of band 3 and adducin in alpha-spectrin-deficient red cells.Protein 4.2 binds to the carboxyl-terminal EF-hands of erythroid alpha-spectrin in a calcium- and calmodulin-dependent manner.Spectraplakins: master orchestrators of cytoskeletal dynamics.Dynamic Regulation of α-Actinin's Calponin Homology Domains on F-Actin Brain spectrin binding to the NMDA receptor is regulated by phosphorylation, calcium and calmodulin.Intertwined αβ spectrin meeting helical actin protofilament in the erythrocyte membrane skeleton: wrap-around vs. point-attachment.

P2860

Q24616347-4DAEDC49-37AA-4F80-9B1F-6BB28AC3A3F0 Q27345234-D238970F-1C6E-4E75-9553-265D09D802AE Q27653516-C41D883A-7EC7-48B2-8F56-81518E7DAD05 Q28512479-E6F61C55-BA62-4C33-BE90-B62B4DD8DAC5 Q33706340-C6E2EA78-F065-4A98-936C-9E9D04585C64 Q33717604-2181482D-0827-4FC4-BF4F-7EF2B5B4EBF0 Q35962308-CD20780F-1104-4BB2-BFBA-49048464BBEC Q36753948-DDDA443C-2CF5-4D17-8633-212F58C5A32D Q41843224-4F49C458-468F-4FB6-8DF7-AD4FB1CDA054 Q41857033-CC82CE52-E3ED-4950-9473-ED231AA86218

P2860

Molecular mechanism of the calcium-induced conformational change in the spectrin EF-hands.

http://www.wikidata.org/entity/Q40789626

description

1995 nî lūn-bûn

@nan

1995年の論文

@ja

1995年学术文章

@wuu

1995年学术文章

@zh-cn

1995年学术文章

@zh-hans

1995年学术文章

@zh-my

1995年学术文章

@zh-sg

1995年學術文章

@yue

1995年學術文章

@zh

1995年學術文章

@zh-hant

name

Molecular mechanism of the cal ...... ange in the spectrin EF-hands.

@en

type

label

Molecular mechanism of the cal ...... ange in the spectrin EF-hands.

@en

prefLabel

Molecular mechanism of the cal ...... ange in the spectrin EF-hands.

@en

P1433

Q40789626-548440B6-657D-40DB-A1E2-88A32474DAAC

P1476

Q40789626-724824C2-AC28-489A-B0B0-ADB3E070FB35

P2093

Q40789626-29EAB86B-2057-40C7-A48B-CEEDAFB2F8A5

Q40789626-9D965916-9DEC-4A7C-824E-3F1774443D9E

Q40789626-A9A0DC87-5E18-4214-9781-1A2990BC7CB3

Q40789626-AE4C99E7-CF94-4432-A5B0-1A3BA6C1F202

P2860

Q40789626-0EA61B69-E755-44D4-83B0-2AC7CC735EE5

Q40789626-17AD4907-4A93-4D04-8F7A-7F6FD8830C18

Q40789626-1CB09A75-D790-4C67-872F-3B184B3A33AE

Q40789626-29139826-248E-4A2A-9FF6-FE5F14918A51

Q40789626-4596F6B5-38AE-4569-825B-8CF8B90318B4

Q40789626-55FC6C30-392B-4FAE-B1E5-2C249B1A9414

Q40789626-6B2DDA5E-1D74-456A-B194-BAFE5B0A3AC4

Q40789626-6F00C29B-BCC9-414B-86C3-DEECB38AD575

Q40789626-88987C7C-DF1A-49C1-9442-8850CDA90955

Q40789626-8AEF2435-AC7F-4300-91D2-CA965E2A0442

P304

Q40789626-63621A94-EEEC-4C2A-A38E-D28887F0EE56

P31

Q40789626-80033E81-C764-4059-900A-5BCC8C0EB67E

P356

Q40789626-ACE68F02-7815-43F0-8ED0-B81F46CF8A65

P407

Q40789626-855ADA2E-1274-45E6-A65D-C0D6E14CD8FC

P433

Q40789626-3C441B05-6749-49A5-B76D-29968A70E908

P478

Q40789626-E2C6B963-06F8-4089-9967-5955E32ED605

P50

Q40789626-5D0CCF63-0295-40F6-903E-445ABCED4F3C

P577

Q40789626-4F0EAC40-B2C3-4017-9993-814D20FD908D

P698

Q40789626-77F6F3D9-5354-4000-9F2B-6873A0EF8C07

P932

Q40789626-602E22EF-A7F8-47B7-BE1D-A139E6ADE548

P356

J.1460-2075.1995.TB00175.X

P1433

The EMBO Journal

P1476

Molecular mechanism of the calcium-induced conformational change in the spectrin EF-hands

@en

P2093

Lacombe PJ

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

Pastore A

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

Saraste M

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

Travé G

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

P2860

WHAT IF: a molecular modeling and drug design program

Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions

Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

Crystal structures of the helix-loop-helix calcium-binding proteins

The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy

Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA

Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.

A model for the Ca2+-induced conformational transition of troponin C. A trigger for muscle contraction.

Three-dimensional structure of calmodulin.

Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex.

P304

4922-4931

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

P31

scholarly article

P356

10.1002/J.1460-2075.1995.TB00175.X

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

P407

P433

20

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

P478

14

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

P50

P577

1995-10-01T00:00:00Z

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

P698

7588621

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

P932

394594

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