Proteasome inhibition enhances the induction and impairs the maintenance of late-phase long-term potentiation. - Wikidata - wikimedia - TriplyDB

Proteasome inhibition enhances the induction and impairs the maintenance of late-phase long-term potentiation.

Proteasome inhibition enhances the induction and impairs the maintenance of late-phase long-term potentiation.

http://www.wikidata.org/entity/Q36625561

about

The roles of protein expression in synaptic plasticity and memory consolidation Protein degradation and protein synthesis in long-term memory formation.The ubiquitin-proteasome system as a critical regulator of synaptic plasticity and long-term memory formation Roles of the ubiquitin proteasome system in the effects of drugs of abuse Age-dependent neuroinflammation and cognitive decline in a novel Ala152Thr-Tau transgenic mouse model of PSP and AD.The right time to learn: mechanisms and optimization of spaced learning The rates of protein synthesis and degradation account for the differential response of neurons to spaced and massed training protocols Phosphorylation of Rpt6 regulates synaptic strength in hippocampal neurons The ubiquitin-specific protease 14 (USP14) is a critical regulator of long-term memory formation.Regulation of the proteasome by neuronal activity and calcium/calmodulin-dependent protein kinase II.Dynamics of Hippocampal Protein Expression During Long-term Spatial Memory Formation The Role of Proteases in Hippocampal Synaptic Plasticity: Putting Together Small Pieces of a Complex Puzzle.The ubiquitin-proteasome pathway and synaptic plasticity.Ubiquitination acutely regulates presynaptic neurotransmitter release in mammalian neurons Protein homeostasis and synaptic plasticity Role of ubiquitin-proteasome-mediated proteolysis in nervous system disease.An essential postsynaptic role for the ubiquitin proteasome system in slow homeostatic synaptic plasticity in cultured hippocampal neurons.Local ubiquitin-proteasome-mediated proteolysis and long-term synaptic plasticity.Proteasome regulates the mediators of cytoplasmic polyadenylation signaling during late-phase long-term potentiation.Ubiquitination in postsynaptic function and plasticity Proteasome regulates transcription-favoring histone methylation, acetylation and ubiquitination in long-term synaptic plasticity.Loss of F-box only protein 2 (Fbxo2) disrupts levels and localization of select NMDA receptor subunits, and promotes aberrant synaptic connectivity.Persistent Associative Plasticity at an Identified Synapse Underlying Classical Conditioning Becomes Labile with Short-Term Homosynaptic Activation.Long-lasting hyperexcitability induced by depolarization in the absence of detectable Ca2+ signals.Further evidence for an anti-inflammatory role of artesunate in experimental cerebral malaria Think locally: control of ubiquitin-dependent protein degradation in neurons The role of the ubiquitin proteasome system in ischemia and ischemic tolerance.Mechanisms governing the reactivation-dependent destabilization of memories and their role in extinction.Proteasome modulates positive and negative translational regulators in long-term synaptic plasticity.Persistent long-term facilitation at an identified synapse becomes labile with activation of short-term heterosynaptic plasticity.Protein degradation and memory formation.Scaffolding proteins of the post-synaptic density contribute to synaptic plasticity by regulating receptor localization and distribution: relevance for neuropsychiatric diseases.ATF4: a Novel Potential Therapeutic Target for Alzheimer's Disease.HECT-type E3 ubiquitin ligases in nerve cell development and synapse physiology.Temporal phases of long-term potentiation (LTP): myth or fact?The Drosophila LC8 homologue Cut-up specifies the axonal transport of proteasomes.Perturbed proteostasis in autism spectrum disorders.Proteolysis, synaptic plasticity and memory.Recent insights on principles of synaptic protein degradation A mammalian nervous-system-specific plasma membrane proteasome complex that modulates neuronal function.

P2860

Q26825627-7F8440C2-D82F-4F38-8773-202058EDFA72 Q26830414-159958E8-5072-4574-A4B9-1EACF6AF91AB Q26865271-F8EB3F5C-D4E6-4345-B46F-4C7E8BB8B569 Q27011348-9C1D8B38-66F2-42D1-994B-59B6D6427679 Q27317039-718F6C95-B9CE-428F-9AC5-D8D566169F4C Q28072871-AE48AC96-C453-4BA7-B478-75C19AAE136B Q28478627-96FDA8C3-0C20-470A-8C97-47210121734F Q28579831-26EBBDF0-9E02-4EDD-8725-F77DB5B82683 Q30421989-96E61CBD-DB64-4D9C-8BBC-9F09113C4AEC Q30492045-FAC3C2D5-6E26-4DF9-9121-C5BD6649BA79 Q30706228-FEED7132-04F0-4811-ABB1-49A6C7DBBB85 Q33361879-3C85A648-B0E5-4374-9507-887085819B6E Q33994715-EF3332F2-18B2-41FB-A18C-42B42C991E72 Q34001940-5DB8838F-097F-4B78-9773-EB88B281BA5B Q34076257-3E1FEF6D-5C0E-49AD-A6E3-13003A502970 Q34372681-9D8A0C90-3AA0-49EB-9265-DFAE8E689A45 Q34509136-E8A3F9B8-5F2F-47D5-8F02-5A51D4BA1271 Q34593368-9EDD89F5-59ED-418B-8499-1601F41D788C Q34615714-B2113E37-E57A-40EF-B3E6-274D347A2BBC Q35186220-8CC519CF-7B23-4D86-BFFE-6EC04C9B2393 Q35186816-C024B3A0-09FB-4EC4-902D-BB2B9EA24063 Q35423787-47CC996E-D858-4841-81BC-6A24A90C4322 Q36380918-74485D35-495D-4B42-8993-BF597CF4F554 Q37152416-FF980165-296C-40D8-A202-7AF54949E2DD Q37306230-96568F23-B04B-4953-A7AC-F00F418CFAD0 Q37349687-5842AAAE-EFAE-47C2-8C92-032624C5EA34 Q37381217-CF421555-6F6F-4D22-9137-F2D3B500F1B3 Q37414015-2F034D06-D3B8-4612-A4F3-8EB3091FFE36 Q37603760-6D078EA8-D4DA-4783-8048-6E9258692065 Q37679288-3B3664C8-4354-404F-B8ED-AE31729B0B6E Q37809597-B0FC9B25-CF54-430F-8FBA-F8C1B2352333 Q38044699-DF332813-8058-4434-8458-61D4CFA07133 Q38266261-A4B1E499-6994-43FF-BEBB-60E7DB78B6CF Q38483115-83FACB03-204D-4050-BB38-094EFB438BC8 Q38493634-BDA75DF4-70A0-45CB-B807-FF0E635011B6 Q38624997-999A4569-F8BC-4DFA-A26A-1D9EB00B3E03 Q38882773-8185B1F3-DD25-4292-BF7A-A38D17E1B364 Q38950862-3C869CE9-2C5B-42A8-B107-C9E043BA031C Q39377253-5FEA5A61-3160-4132-B2D4-D430593AF0E6 Q41757716-DEB27097-9909-46F0-820F-6CAA6F7C96D2

P2860

Proteasome inhibition enhances the induction and impairs the maintenance of late-phase long-term potentiation.

http://www.wikidata.org/entity/Q36625561

description

2008 nî lūn-bûn

@nan

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

2008年论文

@zh

2008年论文

@zh-cn

name

Proteasome inhibition enhances ...... -phase long-term potentiation.

@ast

Proteasome inhibition enhances ...... -phase long-term potentiation.

@en

type

label

Proteasome inhibition enhances ...... -phase long-term potentiation.

@ast

Proteasome inhibition enhances ...... -phase long-term potentiation.

@en

prefLabel

Proteasome inhibition enhances ...... -phase long-term potentiation.

@ast

Proteasome inhibition enhances ...... -phase long-term potentiation.

@en

P1433

Q36625561-7B9F818C-799E-4791-A6BD-D9317F9A9BD9

P1476

Q36625561-8D633B9F-7761-49AC-8390-B0D4FF49C7E6

P2093

Q36625561-0987EA95-8441-4E9F-BAE3-48633DC0EBCD

Q36625561-495163B2-4B08-4A65-B0FE-77D1EC52864D

Q36625561-4ABAC28C-87EF-483F-A886-DD7571B40D4D

Q36625561-9A01E890-9670-4B9D-A2F0-07E5DC836DC2

Q36625561-DA9EBE6F-B8ED-4C4B-AE8B-673C1AD8CFCE

P2860

Q36625561-00523246-72E7-4EC1-A938-9643F7292389

Q36625561-018AB102-54A0-4100-B9E5-7D6C6574098D

Q36625561-025A03DB-F3BE-4267-A72D-54B0D8C2642D

Q36625561-02AF7EFD-4557-4C4E-93A5-CDA6DD4B1820

Q36625561-042E0B32-E751-4622-AE5E-7BC4C666E2A8

Q36625561-064CE08A-D22C-4432-B26B-A6BF667B187F

Q36625561-082B5902-AAF7-441B-9F4C-5B7257F13C72

Q36625561-10F2BB6C-390C-4CE8-9331-9C3D68C8EFF8

Q36625561-12E2566C-C214-4580-A1A1-B39AE24B6D29

Q36625561-1B3654F5-342D-4EA7-881D-E5A242EF4BB0

P304

Q36625561-E8C47679-E485-4E3D-8829-D60597A6ECA1

P31

Q36625561-E2889170-359B-41E9-B4C1-7F971BBFC789

P356

Q36625561-046432BE-531F-4D6E-9AFC-6435D5845FC8

P433

Q36625561-1E1D27D2-CF53-496E-AB1D-D561ABA3C98E

P478

Q36625561-78A7B757-EB47-4D19-8BEC-F4946FFC277D

P577

Q36625561-942C0875-93DB-445B-80C2-C05E8C4A7C73

P5875

Q36625561-CF2F71CF-D7A2-429A-9CCD-3AAA3A218998

P698

Q36625561-107FAD8F-AE72-4AD3-9D7C-24310AF855AC

P932

Q36625561-91B5B300-07BE-4D01-B6FF-3B8875138C11

P356

P1433

Learning and Memory

P1476

Proteasome inhibition enhances ...... -phase long-term potentiation.

@en

P2093

Ashok N Hegde

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

Chenghai Dong

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

Lan Ding

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

Sudarshan C Upadhya

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

Thuy K Smith

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

P2860

ATF4 degradation relies on a phosphorylation-dependent interaction with the SCF(betaTrCP) ubiquitin ligase

Poly(A) binding protein (PABP) homeostasis is mediated by the stability of its inhibitor, Paip2

Influence of actinomycin D, a RNA synthesis inhibitor, on long-term potentiation in rat hippocampal neurons in vivo and in vitro

Tests of the roles of two diffusible substances in long-term potentiation: evidence for nitric oxide as a possible early retrograde messenger

Time-restricted role for dendritic activation of the mTOR-p70S6K pathway in the induction of late-phase long-term potentiation in the CA1

New roles for ubiquitin in the assembly and function of neuronal circuits

Translational control by MAPK signaling in long-term synaptic plasticity and memory

Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin

Increasing numbers of synaptic puncta during late-phase LTP: N-cadherin is synthesized, recruited to synaptic sites, and required for potentiation

Translational control of hippocampal synaptic plasticity and memory by the eIF2alpha kinase GCN2

P304

335-347

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

P31

scholarly article

P356

10.1101/LM.984508

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

P433

5

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

P478

15

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

P577

2008-04-25T00:00:00Z

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

P5875

5411688

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

P698

18441292

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

P932

2364605

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