The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules. - Wikidata - wikimedia - TriplyDB

The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules.

The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules.

http://www.wikidata.org/entity/Q33697630

about

The Metamorphic Nature of the Tau Protein: Dynamic Flexibility Comes at a Cost Proteomics in Traditional Chinese Medicine with an Emphasis on Alzheimer's Disease FKBP51 and FKBP52 in signaling and disease High-resolution crystal structure of FKBP12 from Aedes aegypti Small molecule Plasmodium FKBP35 inhibitor as a potential antimalaria agent Crystal structure and conformational flexibility of the unligated FK506-binding protein FKBP12.6 Crystal structure of Plasmodium vivax FK506-binding protein 25 reveals conformational changes responsible for its noncanonical activity Two crystal structures of the FK506-binding domain of Plasmodium falciparum FKBP35 in complex with rapamycin at high resolution The emerging role of peptidyl-prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's disease The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer's Disease A new anti-depressive strategy for the elderly: ablation of FKBP5/FKBP51.Association of FKBP51 with priming of autophagy pathways and mediation of antidepressant treatment response: evidence in cells, mice, and humans The helix 1-3 loop in the glucocorticoid receptor LBD is a regulatory element for FKBP cochaperones.The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases Differential conformational dynamics in the closely homologous FK506-binding domains of FKBP51 and FKBP52.Hsc70 rapidly engages tau after microtubule destabilization Age-associated epigenetic upregulation of the FKBP5 gene selectively impairs stress resiliency.Loss of Hsp110 leads to age-dependent tau hyperphosphorylation and early accumulation of insoluble amyloid beta.The diarylheptanoid (+)-aR,11S-myricanol and two flavones from bayberry (Myrica cerifera) destabilize the microtubule-associated protein tau.The Hsp90 kinase co-chaperone Cdc37 regulates tau stability and phosphorylation dynamics.Organization and function of the FKBP52 and FKBP51 genes.Management of cytoskeleton architecture by molecular chaperones and immunophilins.Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies.Endoplasmic reticulum stress or mutation of an EF-hand Ca(2+)-binding domain directs the FKBP65 rotamase to an ERAD-based proteolysis Impact of genetic variation in FKBP5 on clinical response in pediatric acute myeloid leukemia patients: a pilot study.Increased cortical expression of FK506 binding protein-51 in HIV-associated neurocognitive disorders Cdc37/Hsp90 protein complex disruption triggers an autophagic clearance cascade for TDP-43 protein Primate-specific melanoma antigen-A11 regulates isoform-specific human progesterone receptor-B transactivation.Analysis of the tau-associated proteome reveals that exchange of Hsp70 for Hsp90 is involved in tau degradation Gene-Stress-Epigenetic Regulation of FKBP5: Clinical and Translational Implications Imbalance of Hsp70 family variants fosters tau accumulation.Mice devoid of Tau have increased susceptibility to neuronal damage in myelin oligodendrocyte glycoprotein-induced experimental autoimmune encephalomyelitis.Identification of Novel Tau Interactions with Endoplasmic Reticulum Proteins in Alzheimer's Disease Brain.Tau accumulation activates the unfolded protein response by impairing endoplasmic reticulum-associated degradation Expression and localization of the immunophilin FKBP51 in colorectal carcinomas and primary metastases, and alterations following oxaliplatin-based chemotherapy Stressing Out Hsp90 in Neurotoxic Proteinopathies.Accelerated neurodegeneration through chaperone-mediated oligomerization of tau.The FKBP5 Gene Affects Alcohol Drinking in Knockout Mice and Is Implicated in Alcohol Drinking in Humans.The Mechanistic Links Between Proteasome Activity, Aging and Age-related Diseases.Tau protein modifications and interactions: their role in function and dysfunction.

P2860

Q26772846-FB3ECCB2-B3F1-426D-B8E4-978CC24A88C3 Q26777933-9F0937C2-21C9-4B63-8A25-FDE36321EB02 Q26861304-C10B478C-531E-4FD4-A5E7-A57EBEE23882 Q27678624-21A4B61E-56D9-44E5-A6DE-5CF4961AA79B Q27679795-D92CFBE2-3EF9-4D26-91B1-D4510773FDC3 Q27681988-875146CB-D2E4-4173-A2B8-046C8284206F Q27687798-92EFB7E7-E4AF-4FDC-96D2-BDEF98F1F4C7 Q27700988-92DAEA51-51EF-4171-8414-C1EB33EE0DE0 Q28085108-9932D270-E8B8-467C-BED2-249A27E088FC Q28254943-6E7119B7-89CE-421B-AA26-30E415358954 Q28477103-C75F06FD-0CB8-4ACD-9697-5CA1AF6137A2 Q28544844-DED5DEE9-E7F8-436F-A71C-34705C1515BF Q33633104-65DD1785-93BB-4C27-ABD0-048E26A058DD Q33692255-696B06DE-411E-4337-A0B2-9D1DA9DB89EA Q33768592-5A622923-90DE-47BD-9F9F-713A6024DB42 Q33883285-7929F30B-0E85-42EB-A8FF-8C227162B8D1 Q34142685-07311CDF-EF91-4F7D-B055-199047858BD1 Q34177990-CDDD5407-AF85-4C27-9D16-9EFE0D4DADC6 Q34761869-CCC34629-0686-4AA4-A00E-42C02B0D3AC1 Q34947846-0620D613-DE68-4AB9-90A9-8FA2CEBF8004 Q35165005-87D07702-19C7-43E3-A3B8-52ED908D126E Q35250454-EB0B6706-0696-4ACA-BB62-92BF9926BFE6 Q35313148-74744775-BC7D-41D2-A03D-03CF3AA6320B Q35562258-9C06B3C3-CB7E-46D6-81DE-9E7F320736DC Q35615051-E5DFDBE8-333C-4155-B1F1-915EB0909C7A Q36031037-CC5149DC-9016-4718-B6BF-6C585BCF6D80 Q36098117-FEC62032-5EC1-44EE-AF03-A46D94EC809F Q36298532-3D20696C-A7E9-42D4-BBC3-EE4D9416A206 Q36335851-123BC0F1-F175-4F67-BA35-FF8189E498E0 Q36366772-DF506A84-23FD-456F-872B-294D8A121420 Q36710912-67832818-270E-4FA7-B262-85420C338E66 Q36768844-BB8ED8A4-AE3C-40BC-9901-8C0C128ED44E Q36939900-91FBC873-7E28-41FC-A606-A31C08583A34 Q37069517-BFB28DCA-9A2E-45E0-A4F9-1347A41718B5 Q37108510-2CA5F4D9-95AD-4230-828D-16D96D02441F Q37198079-744DAFCC-8D29-40C8-88F5-EB37EE0B7041 Q37200867-63122649-3086-444E-87BC-30E26A9195B1 Q37210025-DFDFBBDD-5DAE-46AF-92DC-316716CF6BB8 Q37645630-BB30D03E-7A5C-4EA2-ABE8-E64C2D5242B3 Q37684106-CEB7E709-5822-447E-879F-820E50A6F2D9

P2860

The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules.

http://www.wikidata.org/entity/Q33697630

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules.

@ast

The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules.

@en

type

label

The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules.

@ast

The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules.

@en

prefLabel

The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules.

@ast

The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules.

@en

P1433

Q33697630-D63006B3-FAD2-47C4-A033-FE88AA4E0401

P1476

Q33697630-E0AF61CE-B439-4EB5-8396-4863D6DFB9E1

P2093

Q33697630-014F4133-7CAF-4F7D-9122-2A3B9D674EF5

Q33697630-2A2B2C89-8DAC-43FA-9565-470333EBBE4B

Q33697630-3D4E627C-DAD8-4570-B1ED-C98A87FA3D9F

Q33697630-677CABCF-25B0-49AD-B632-0DDBAF329B9A

Q33697630-75FB6126-54AF-4966-89CA-19C67E317141

Q33697630-AE7F7251-8765-4D42-B366-7C60877FA881

Q33697630-C67EA2E5-401F-41C2-B881-FFCC8F73FD87

Q33697630-D3B3C060-5987-424F-9616-7C250AA9FB94

Q33697630-D675F0AD-6138-4568-A099-2C460C9D43F0

Q33697630-DD60D9CC-A450-475F-96B0-1581B0C5AB26

P2860

Q33697630-010AD640-11F2-4DA9-8607-B2FCF0C0F572

Q33697630-07C665BB-4046-492B-8883-F563EA4918F0

Q33697630-0B56690A-807B-4233-A673-EED692B12F8F

Q33697630-13253CF6-925A-41BB-A708-C43ADBFF703C

Q33697630-19B43065-B75F-42CD-B4C2-6DBE8DD0BA1D

Q33697630-32D9EC99-CFC9-41B6-8E94-4053FDC84916

Q33697630-34372958-3149-4235-9C8B-0C4820DC2373

Q33697630-489EFA11-6772-4A4A-BA5B-FCD748AF179D

Q33697630-5684CDC3-1463-4255-B1A6-6A0CE231D167

Q33697630-5C57DD7E-44C2-4327-8857-D68B9CBBBF58

P304

Q33697630-0D77B6A6-4570-4742-8D8B-71EDB8833DAC

P31

Q33697630-579232A0-EF2E-4438-B540-1E438816B417

P356

Q33697630-3E43EE6E-00E1-466B-B863-FC08CF513AB0

P407

Q33697630-1FD2C39F-1D5F-4445-84DA-37FDD102601A

P433

Q33697630-F2540A9A-EF23-4582-B809-4849077F0DB7

P478

Q33697630-6C3248E7-A74C-4FE3-8276-6BEC64752BDF

P50

Q33697630-3B24E172-EA66-4540-AD0A-85955B51F0CB

Q33697630-7DA9C07C-FB5C-4B1F-9775-81496F98C6A9

Q33697630-8F0B4811-F24D-4E24-AEAA-2B0C94ADD2F3

Q33697630-DEB12C69-E45C-4337-9D6D-D8F88FB27B4A

P577

Q33697630-3FA998ED-5E8E-4DA3-B1DE-449886DE15A0

P698

Q33697630-00E696B6-957A-4919-970F-192DF70C9840

P932

Q33697630-B58C1A6F-969C-4878-9640-C31937F5ADD8

P356

JNEUROSCI.4815-09.2010

P1433

Journal of Neuroscience

P1476

The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules

@en

P2093

Amelia G Johnson

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

Andreas B Schmid

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

Chad A Dickey

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

Cody L Shults

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

Johannes Buchner

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

John C O'Leary

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

Jose F Abisambra

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

Sergiy I Borysov

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

Umesh K Jinwal

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

Ying Jin

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

P2860

Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40

Identification of VCP/p97, carboxyl terminus of Hsp70-interacting protein (CHIP), and amphiphysin II interaction partners using membrane-based human proteome arrays

The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production

Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis

Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4

Akt and CHIP coregulate tau degradation through coordinated interactions

Calculation of protein extinction coefficients from amino acid sequence data

Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1

The tetratricopeptide repeat: a structural motif mediating protein-protein interactions

Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides

P304

591-599

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

P31

scholarly article

P356

10.1523/JNEUROSCI.4815-09.2010

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

P407

P433

2

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

P478

30

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

P50

P577

2010-01-01T00:00:00Z

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

P698

20071522

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

P932

2830818

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