An ultrasensitive Ca2+/calmodulin-dependent protein kinase II-protein phosphatase 1 switch facilitates specificity in postsynaptic calcium signaling - Test2 - elhamkhani - TriplyDB

An ultrasensitive Ca2+/calmodulin-dependent protein kinase II-protein phosphatase 1 switch facilitates specificity in postsynaptic calcium signaling

An ultrasensitive Ca2+/calmodulin-dependent protein kinase II-protein phosphatase 1 switch facilitates specificity in postsynaptic calcium signaling

http://www.wikidata.org/entity/Q24683178

about

Calcium input frequency, duration and amplitude differentially modulate the relative activation of calcineurin and CaMKII Design of versatile biochemical switches that respond to amplitude, duration, and spatial cues The stability of a stochastic CaMKII switch: dependence on the number of enzyme molecules and protein turnover CaMKII tethers to L-type Ca2+ channels, establishing a local and dedicated integrator of Ca2+ signals for facilitation Counteracting Protein Kinase Activity in the Heart: The Multiple Roles of Protein Phosphatases Modeling intracellular signaling underlying striatal function in health and disease Mechanisms of CaMKII action in long-term potentiation Intersubunit capture of regulatory segments is a component of cooperative CaMKII activation Role of DARPP-32 and ARPP-21 in the Emergence of Temporal Constraints on Striatal Calcium and Dopamine Integration Subcellular location of PKA controls striatal plasticity: stochastic simulations in spiny dendrites A model of late long-term potentiation simulates aspects of memory maintenance A kinetic model of dopamine- and calcium-dependent striatal synaptic plasticity Calcium/calmodulin dependent protein kinase II bound to NMDA receptor 2B subunit exhibits increased ATP affinity and attenuated dephosphorylation Computational investigation of the changing patterns of subtype specific NMDA receptor activation during physiological glutamatergic neurotransmission Protection of α-CaMKII from Dephosphorylation by GluN2B Subunit of NMDA Receptor Is Abolished by Mutation of Glu96 or His282 of α-CaMKII Complete integrability of information processing by biochemical reactions Calmodulin mediates differential sensitivity of CaMKII and calcineurin to local Ca2+ in cardiac myocytes Ultrasensitive response motifs: basic amplifiers in molecular signalling networks.The CaMKII holoenzyme structure in activation-competent conformations Experimental and computational aspects of signaling mechanisms of spike-timing-dependent plasticity.Detailed state model of CaMKII activation and autophosphorylation.The effect of noise on CaMKII activation in a dendritic spine during LTP induction Muscle-type specific autophosphorylation of CaMKII isoforms after paced contractions.Regulation of cytoplasmic polyadenylation can generate a bistable switch.CaMKII activation and dynamics are independent of the holoenzyme structure: an infinite subunit holoenzyme approximation Postsynaptic depolarization requirements for LTP and LTD: a critique of spike timing-dependent plasticity.A model of the roles of essential kinases in the induction and expression of late long-term potentiation.The roles of Ca2+, downstream protein kinases, and oscillatory signaling in regulating fertilization and the activation of development.Kinetic memory based on the enzyme-limited competition Targeting of calcium/calmodulin-dependent protein kinase II.MAPK feedback encodes a switch and timer for tunable stress adaptation in yeast.Calcium specificity signaling mechanisms in abscisic acid signal transduction in Arabidopsis guard cells Control of βAR- and N-methyl-D-aspartate (NMDA) Receptor-Dependent cAMP Dynamics in Hippocampal Neurons.Dendritic sodium spikes are required for long-term potentiation at distal synapses on hippocampal pyramidal neurons.Increased neuronal activity fragments the Golgi complex.Calmodulin and CaMKII as molecular switches for cardiac ion channels.Negative regulation of multifunctional Ca2+/calmodulin-dependent protein kinases: physiological and pharmacological significance of protein phosphatases.Dissecting cooperative calmodulin binding to CaM kinase II: a detailed stochastic model Molecular mechanism of activation-triggered subunit exchange in Ca(2+)/calmodulin-dependent protein kinase II Role(s) of the serine/threonine protein phosphatase 1 on mammalian sperm motility.

P2860

Q21134074-1F360047-F9F2-4D4C-9520-210A94548E9E Q24646003-84EC1693-E99A-4481-AFD9-9F0983FF5CEA Q24805203-13F70E96-E212-4EB3-BFF0-A33DFDE82F55 Q25255889-FCA0B2A6-039D-4AF7-A386-E38CF853177A Q26776182-D2BDEB55-BAE6-45BB-9464-7CFED2D140FA Q26851389-1D560EBD-2E4F-4D40-B440-12B4B1E651A9 Q26998387-E35C0E4B-2A06-4D0D-B9D5-580DE8952AB5 Q27659633-B63BE33C-C71E-4F60-A485-5653DEA4DB66 Q28388265-84CE5F72-CA8E-4269-B453-E126D5DF40C4 Q28396564-6B22E7A8-88F8-40C4-8002-CA4404459625 Q28469200-AA79494E-109F-4825-9645-4664DE7F349F Q28472858-149F829F-4089-4315-8BF8-8D7F40289543 Q28477424-CA1F4EE7-BA29-429F-A341-5CE484FC3EC9 Q28478887-C5A68440-7216-4510-8C6B-ECBDC5D2A321 Q28554007-0DA5597B-3614-47E3-A8EB-15871F0F9961 Q28822181-90AB33C1-A635-4B7E-B11C-010A97E24FF5 Q30437877-D68CE423-B215-402A-BDED-43E96E8D5C9F Q30541676-03293BB4-F743-4F87-BDDB-7719CAE54259 Q30855420-00421694-9ACF-4136-B430-B79B2A3FBC94 Q33565311-0E1B75AE-9F67-438C-9EF4-B41B9029EB02 Q33572062-24BC3BFA-B1B4-4F93-BE6F-D29D0447B8AD Q33783785-959D6376-EFDA-45CF-85EA-C44BC248BDB8 Q33904592-7ED94B53-3E72-45A7-8C38-87238A18F81F Q34159458-33A809FD-11DB-4F1E-9681-C5AAE7D37117 Q34280253-A8CFFCF8-523C-4906-A3FA-FC9FA1E27D74 Q34447669-C39D2C32-7119-4135-A913-D710F77D597E Q34481520-BC86FDD3-7F2F-4FFB-B40F-838227B08104 Q34769299-CE0782A0-AF1E-4AF2-96FF-9B6276361B13 Q35224716-CB980E77-150D-4DA0-B3A0-31991219E923 Q35599584-90D21A2D-C922-4E5A-BE47-A7F12B28AC3B Q35861696-3A5AE261-C2A3-416B-9FED-DC510017E1F2 Q35866896-C193A8B0-C784-4607-997C-262AA69A6201 Q35931515-6C3424DF-A998-48FE-BD68-0AEDBADF0602 Q36076161-53FE5FC3-DD9D-48C1-B7F9-F258BF310392 Q36567791-2A1CB7D2-F736-4E0D-8A56-8454922309CE Q36669731-D4740DF7-C411-43B9-9F3B-C2CA1A501056 Q36736320-D5CCB11C-DAF3-43C9-9734-6E074CB8AEFB Q36741607-B48E0BDF-05D2-4B25-9176-4862C2B39586 Q36879246-67AA0A3C-DC51-403D-B6C3-91BBFE808487 Q36939450-61787867-4C97-40DD-A05C-EB066CE41D03

P2860

An ultrasensitive Ca2+/calmodulin-dependent protein kinase II-protein phosphatase 1 switch facilitates specificity in postsynaptic calcium signaling

http://www.wikidata.org/entity/Q24683178

description

2003 nî lūn-bûn

@nan

2003 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

An ultrasensitive Ca2+/calmodu ...... postsynaptic calcium signaling

@ast

An ultrasensitive Ca2+/calmodu ...... postsynaptic calcium signaling

@en

An ultrasensitive Ca2+/calmodu ...... postsynaptic calcium signaling

@nl

type

label

An ultrasensitive Ca2+/calmodu ...... postsynaptic calcium signaling

@ast

An ultrasensitive Ca2+/calmodu ...... postsynaptic calcium signaling

@en

An ultrasensitive Ca2+/calmodu ...... postsynaptic calcium signaling

@nl

prefLabel

An ultrasensitive Ca2+/calmodu ...... postsynaptic calcium signaling

@ast

An ultrasensitive Ca2+/calmodu ...... postsynaptic calcium signaling

@en

An ultrasensitive Ca2+/calmodu ...... postsynaptic calcium signaling

@nl

P1433

Q24683178-E1F5B767-217F-495E-A779-7E119F5EB271

P1476

Q24683178-4FA5CED9-CCED-48DB-841C-A322AE040801

P2093

Q24683178-00DB9932-AE03-4FED-87FD-99AB65E3F124

Q24683178-9290EAC1-CB6A-4EC9-B1AC-7CC02F804C17

Q24683178-B7DE709F-F3C0-4798-A509-D80FF1764110

Q24683178-F52850EB-5EFB-4D25-AD8B-7260FA1B085D

P2860

Q24683178-0C794534-BF77-4817-A4A7-1509E8F9BBD3

Q24683178-0F49180B-E3BF-4543-83C5-FF6332BD3A5E

Q24683178-1A173905-152E-4154-8745-AC8666D9C193

Q24683178-366234B2-61BD-468F-9D4D-05F71423A98C

Q24683178-3B9A3D81-1071-4D8C-85AB-0C192753DC2F

Q24683178-3D7CF07D-D857-408A-9833-640AD67CEEB4

Q24683178-49D05110-0964-4B98-AF90-DE8A1702BE83

Q24683178-4DAE5461-0928-4AEE-8ED3-881D2317AC97

Q24683178-5CE72693-95A8-4E42-8001-BBD7E2755608

Q24683178-5FE59A34-9005-4C7F-B559-116EF14A7554

P304

Q24683178-9137E8D9-D03B-49D4-8E08-DC2D0EB90BF0

P31

Q24683178-44860076-EEE0-4677-841A-D529B1791ACB

P3181

Q24683178-AC900752-582B-484A-9304-966AF24EC255

P356

Q24683178-62A569D8-C420-4ED7-84F4-8DCBE5925684

P407

Q24683178-DBE11AD6-BF8A-4EDE-823D-527E9F2398C7

P433

Q24683178-74751181-9644-4F9C-AB6F-F7B71975E193

P478

Q24683178-CAC454F4-E1ED-49A4-96CF-07646DFA5479

P577

Q24683178-309DB4F7-1DEC-45CC-BCD5-CD42D780A512

P5875

Q24683178-5BD31660-025E-4B05-8A8B-7B69F667C8D9

P698

Q24683178-6932A033-39CB-4C6F-9459-8F67352514AD

P932

Q24683178-C7462287-6710-4412-A5AA-23E3D2017236

P3181

P356

PNAS.1932759100

P1433

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

P1476

An ultrasensitive Ca2+/calmodu ...... postsynaptic calcium signaling

@en

P2093

Howard Schulman

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

J Michael Bradshaw

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

Tobias Meyer

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

Yoshi Kubota

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

P2860

Neuronal CA2+/calmodulin-dependent protein kinase II: the role of structure and autoregulation in cellular function

The molecular basis of CaMKII function in synaptic and behavioural memory

Autophosphorylation at Thr286 of the alpha calcium-calmodulin kinase II in LTP and learning

Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation

Cellular signaling through multifunctional Ca2+/calmodulin-dependent protein kinase II.

Bistability in the Ca(2+)/calmodulin-dependent protein kinase-phosphatase system

A mechanism for the Hebb and the anti-Hebb processes underlying learning and memory.

A model of synaptic memory: a CaMKII/PP1 switch that potentiates transmission by organizing an AMPA receptor anchoring assembly.

How regulated protein translocation can produce switch-like responses.

A fresh look at the role of CaMKII in hippocampal synaptic plasticity and memory.

P304

10512-7

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

P31

scholarly article

P3181

2605511

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

P356

10.1073/PNAS.1932759100

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

P407

P433

18

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

P478

100

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

P577

2003-09-02T00:00:00Z

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

P5875

10604928

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

P698

12928489

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

P932

193592

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