Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity - Test2 - elhamkhani - TriplyDB

Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity

Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity

http://www.wikidata.org/entity/Q24679238

about

Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control Sox17 and Sox4 differentially regulate beta-catenin/T-cell factor activity and proliferation of colon carcinoma cells TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in the brain of Parkinson's disease and dementia with Lewy bodies Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle Wnt-5a inhibits the canonical Wnt pathway by promoting GSK-3-independent beta-catenin degradation Cells adapted to the proteasome inhibitor 4-hydroxy- 5-iodo-3-nitrophenylacetyl-Leu-Leu-leucinal-vinyl sulfone require enzymatically active proteasomes for continued survival The tumor inhibitor and antiangiogenic agent withaferin A targets the intermediate filament protein vimentin Proteasome inhibition interferes with gag polyprotein processing, release, and maturation of HIV-1 and HIV-2 Binding of LARP6 to the conserved 5' stem-loop regulates translation of mRNAs encoding type I collagen The selective proteasome inhibitors lactacystin and epoxomicin can be used to either up- or down-regulate antigen presentation at nontoxic doses Proteasome inhibition by fellutamide B induces nerve growth factor synthesis A novel mechanism for the regulation of amyloid precursor protein metabolism Selective inhibitors of the osteoblast proteasome stimulate bone formation in vivo and in vitro Functional importance of the anaphase-promoting complex-Cdh1-mediated degradation of TMAP/CKAP2 in regulation of spindle function and cytokinesis.Endoplasmic reticulum degradation impedes olfactory G-protein coupled receptor functional expression Proteasome inhibitors: their effects on arachidonic acid release from cells in culture and arachidonic acid metabolism in rat liver cells Relevance of Endoplasmic Reticulum Stress Cell Signaling in Liver Cold Ischemia Reperfusion Injury Drugging the undruggables: exploring the ubiquitin system for drug development From epoxomicin to carfilzomib: chemistry, biology, and medical outcomes Targeted treatments for multiple myeloma: specific role of carfilzomib Targeting the ubiquitin-proteasome system in heart disease: the basis for new therapeutic strategies The ubiquitin/proteasome system mediates entry and endosomal trafficking of Kaposi's sarcoma-associated herpesvirus in endothelial cells Ubiquitination and proteasomal degradation of interferon regulatory factor-3 induced by Npro from a cytopathic bovine viral diarrhea virus Cytopathic and Noncytopathic Interferon Responses in Cells Expressing Hepatitis C Virus Subgenomic Replicons Synthetic and structural studies on syringolin A and B reveal critical determinants of selectivity and potency of proteasome inhibition Elucidation of the α-keto-aldehyde binding mechanism: a lead structure motif for proteasome inhibition One-shot NMR analysis of microbial secretions identifies highly potent proteasome inhibitor Homopiperazine derivatives as a novel class of proteasome inhibitors with a unique mode of proteasome binding Enzyme Inhibition by Hydroamination: Design and Mechanism of a Hybrid Carmaphycin-Syringolin Enone Proteasome Inhibitor Systematic comparison of peptidic proteasome inhibitors highlights the α-ketoamide electrophile as an auspicious reversible lead motif Selective inhibition of the immunoproteasome by ligand-induced crosslinking of the active site The Role of Panobinostat Plus Bortezomib and Dexamethasone in Treating Relapsed or Relapsed and Refractory Multiple Myeloma: A European Perspective Mechanism of Action of Bortezomib and the New Proteasome Inhibitors on Myeloma Cells and the Bone Microenvironment: Impact on Myeloma-Induced Alterations of Bone Remodeling Pathophysiological processes in multiple sclerosis: focus on nuclear factor erythroid-2-related factor 2 and emerging pathways Proteasome-mediated processing of Nrf1 is essential for coordinate induction of all proteasome subunits and p97 Inhibition of proteasome activity strongly affects kiwifruit pollen germination. Involvement of the ubiquitin/proteasome pathway as a major regulator A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14 The ubiquitin-proteasome pathway and proteasome inhibitors Acute decreases in proteasome pathway activity after inhalation of fresh diesel exhaust or secondary organic aerosol Protein kinase Cdelta stimulates proteasome-dependent degradation of C/EBPalpha during apoptosis induction of leukemic cells

P2860

Q24290224-D368E9EB-95E1-43D7-A05A-F0437C0327D3 Q24294207-6E59E482-5991-45FB-8B6E-ECBC51B32210 Q24296382-4A4233C6-1917-41F0-ADC9-D8533A8860D8 Q24299947-26FAE910-423D-4EBA-BAF7-E99317989513 Q24319714-7EDFEB11-D49D-4719-8662-05C37EC488AD Q24542503-AFF888BA-CD33-4B2C-B6E1-038CCD45F3DC Q24633116-DB8E7F2C-810C-4478-BDB4-53E50D80B699 Q24643016-D4827F1A-9EC9-4D94-8780-9E08180A302B Q24644087-2DC0F61D-B4F2-4D62-A493-D78AE527A68F Q24645843-FBF079E4-9BA7-43DE-A4F0-4DD3FC88682F Q24654152-776070E1-5FE6-4D0C-A5FA-F279F74B0978 Q24674865-C7388B9D-19C1-4891-A79A-AD8D4AE03012 Q24675778-21DDFEB1-3B11-45B9-BA1D-6AF429F00CFC Q24683190-98BE6600-AF4F-4924-A679-C5FA4E1C8ABC Q24795923-A661F2AE-FED0-4C8E-A532-A3249D50BCDC Q24801210-61318E36-265E-4267-B76A-29D483B3B623 Q26745583-D2B88C36-4777-48EA-8B19-A3D99F09D104 Q26752823-A01A649A-6316-4D78-B647-DF9F6C7AD467 Q26864557-D11FAF95-7A61-4F78-9169-764FDB470A10 Q26996524-28144903-EF34-419B-8488-A5F73B7231D2 Q27026951-D2BBA9E6-A25C-41F1-B8A5-6C95CB0340FF Q27345534-428F7F8A-3A22-4B50-BD0F-0028B84ED303 Q27481222-BE69D1D8-26D5-4AC7-A4F2-F60D69B2BACD Q27485424-61595224-F716-485F-9B88-C7A0C7BD30CB Q27654628-DC28CBD4-5190-423B-89CD-44214BFFDB13 Q27666372-365B2388-9A57-4962-BD15-318AB3935EB9 Q27674685-77288E7D-2A83-41DD-864D-F566A0F0D74A Q27677425-7BD0A81F-E7FC-4E19-9751-EC7949CB4F21 Q27684346-34A78E85-FE35-466D-A5F6-3B6D49A89172 Q27688108-C4092E70-EEC0-4648-A2C0-A6A1FB36011D Q27695633-1C055F78-ED8B-4668-AD4A-FE3C209DCEB1 Q28069789-F48ED068-8479-4FE3-BC3F-1938D87985BF Q28082335-D58232A8-E976-46D3-80F5-D41FE341B93C Q28235168-2B38C8A1-7CF0-4BBE-9240-EF1FA5AD91FC Q28243388-DC280628-3612-4E0E-881E-510F5ADD4809 Q28344214-F878F125-8C82-4856-956F-0743AF89A60E Q28359750-A394E75F-2F17-4824-9D37-4BCFEE788D64 Q28367002-10502135-163B-43E1-B380-CEC840E0D207 Q28388522-917E05C4-D0AE-4165-A163-59AD8C285A21 Q28475914-5D3BB1FC-E80B-4CDC-BB63-3AD20397B953

P2860

Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity

http://www.wikidata.org/entity/Q24679238

description

1999 nî lūn-bûn

@nan

1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

1999年の論文

@ja

1999年論文

@yue

1999年論文

@zh-hant

1999年論文

@zh-hk

1999年論文

@zh-mo

1999年論文

@zh-tw

1999年论文

@wuu

name

Epoxomicin, a potent and selec ...... vivo antiinflammatory activity

@ast

Epoxomicin, a potent and selec ...... vivo antiinflammatory activity

@en

Epoxomicin, a potent and selec ...... vivo antiinflammatory activity

@nl

type

label

Epoxomicin, a potent and selec ...... vivo antiinflammatory activity

@ast

Epoxomicin, a potent and selec ...... vivo antiinflammatory activity

@en

Epoxomicin, a potent and selec ...... vivo antiinflammatory activity

@nl

prefLabel

Epoxomicin, a potent and selec ...... vivo antiinflammatory activity

@ast

Epoxomicin, a potent and selec ...... vivo antiinflammatory activity

@en

Epoxomicin, a potent and selec ...... vivo antiinflammatory activity

@nl

P1433

Q24679238-4D5040EF-F3D1-4F34-822F-BB5EC9381D47

P1476

Q24679238-9891777B-7120-4D3E-A11B-F4CF8180C133

P2093

Q24679238-7064B251-C7BC-4CD6-AA0A-2D6CCD370115

Q24679238-7A6FF67F-A555-4D99-9489-E3803304634B

Q24679238-B85DD0F5-578A-4BBB-81E5-21520B2720CF

Q24679238-BA51A42E-3DC1-489A-8AB8-D54A4A16F1D4

Q24679238-D3DAA10F-D9B4-499C-8476-00328B8FDCE2

Q24679238-D68E06A5-CFE5-43B8-B3BA-4BAE2DC0DD5A

P2860

Q24679238-00BE839C-488A-4DEF-BF62-A9AF672B840A

Q24679238-0A245F7F-561A-4F1B-B31B-3DB64573ED37

Q24679238-0A3F5441-4CB5-447A-B017-15C741017A0A

Q24679238-11D4D0B4-4D96-40FF-BF29-FEAAC4419BED

Q24679238-1AF0A2FF-502C-455A-806A-7C08A0EBCBCA

Q24679238-27E0A31C-1EA8-4D0A-89CE-8AFA667C397B

Q24679238-2C5E0B57-8A47-4AC6-93ED-569976CD7688

Q24679238-33281DD6-703D-4332-9171-4505D01EF458

Q24679238-39C0F805-E1EE-4411-BD6A-30DE5097D0B6

Q24679238-3AEEA321-EA57-449E-A19A-97D5DB9AC680

P304

Q24679238-85D0E166-1E82-4434-BEF7-D0BA1261D6BC

P31

Q24679238-7CC39730-9244-4B22-9E6B-1142D8BD71DA

P3181

Q24679238-629F1AC5-D452-4B97-921D-12119CB1D502

P356

Q24679238-539AAB4F-9A7A-460D-B64A-68C601E8CF74

P407

Q24679238-64E6EDE1-583C-474C-874B-D2965C044EEB

P433

Q24679238-A9AD96EC-DDE4-4CD4-9F41-99540CDE215E

P478

Q24679238-DE1819ED-CBE0-408E-9E33-294AB2BF907B

P577

Q24679238-2363B8F6-433D-4969-A4F5-3DF4E88FCCCE

P5875

Q24679238-89EA663D-A939-4014-8639-D5257CCDBABF

P698

Q24679238-1651C72F-F2BE-4C8A-948E-2547D08516D1

P921

Q24679238-F78FE08F-D89A-4F10-A212-75F40C4B7FDB

P932

Q24679238-1FCB3264-D512-4429-826F-8A17735273F2

P3181

P356

PNAS.96.18.10403

P1433

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

P1476

Epoxomicin, a potent and selec ...... vivo antiinflammatory activity

@en

P2093

B H Kwok

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

C M Crews

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

L Meng

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

M Elofsson

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

N Sin

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

R Mohan

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

P2860

A giant protease with potential to substitute for some functions of the proteasome

Structure and functions of the 20S and 26S proteasomes

A proteasome inhibitor prevents activation of NF-kappa B and stabilizes a newly phosphorylated form of I kappa B-alpha that is still bound to NF-kappa B

Structure of 20S proteasome from yeast at 2.4 A resolution

NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses

Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules

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

Epoxomicin, a new antitumor agent of microbial origin

Role of the proteasome and NF-kappaB in streptococcal cell wall-induced polyarthritis

Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain

P304

10403-8

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

P31

scholarly article

P3181

1369951

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

P356

10.1073/PNAS.96.18.10403

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

P407

P433

18

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

P478

96

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

P577

1999-08-31T00:00:00Z

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

P5875

235615908

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

P698

10468620

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

P921

P932

17900

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