Beta 2 subunit propeptides influence cooperative proteasome assembly. - Test2 - elhamkhani - TriplyDB

Beta 2 subunit propeptides influence cooperative proteasome assembly.

Beta 2 subunit propeptides influence cooperative proteasome assembly.

http://www.wikidata.org/entity/Q34161423

about

Immunoproteasome deficiency modifies the alternative pathway of NFκB signaling A mutation in the immunoproteasome subunit PSMB8 causes autoinflammation and lipodystrophy in humans Immunoproteasomes: structure, function, and antigen presentation Molecular architecture and assembly of the eukaryotic proteasome The immunoproteasome and viral infection: a complex regulator of inflammation Proteasome assembly Comparative analysis of transcriptional profiling of CD3+, CD4+ and CD8+ T cells identifies novel immune response players in T-cell activation.Interferon-γ induces immunoproteasomes and the presentation of MHC I-associated peptides on human salivary gland cells.Immunoproteasome deficiency alters retinal proteasome's response to stress Two abundant proteasome subtypes that uniquely process some antigens presented by HLA class I molecules.Elucidating the catalytic subunit composition of distinct proteasome subtypes: a crosslinking approach employing bifunctional activity-based probes.Revealing Missing Human Protein Isoforms Based on Ab Initio Prediction, RNA-seq and Proteomics Denervation-Induced Activation of the Standard Proteasome and Immunoproteasome Proteasome function is not impaired in healthy aging of the lung.The proteasome: overview of structure and functions.The proteasome immunosubunit multicatalytic endopeptidase complex-like 1 is a T-cell-intrinsic factor influencing homeostatic expansion Subcellular distribution and dynamics of active proteasome complexes unraveled by a workflow combining in vivo complex cross-linking and quantitative proteomics.Activity-based imaging probes of the proteasome.Mixed proteasomes function to increase viral peptide diversity and broaden antiviral CD8+ T cell responses Heterogeneous cardiac proteasomes: mandated by diverse substrates?Assembly of the 20S proteasome.Proteasome subtypes and regulators in the processing of antigenic peptides presented by class I molecules of the major histocompatibility complex.A bright approach to the immunoproteasome: development of LMP2/β1i-specific imaging probes.The proteasome immunosubunits, PA28 and ER-aminopeptidase 1 protect melanoma cells from efficient MART-126-35 -specific T-cell recognition.Proteasome Structure and Assembly.PA28 and the proteasome immunosubunits play a central and independent role in the production of MHC class I-binding peptides in vivo.LMP2-specific inhibitors: chemical genetic tools for proteasome biology.Characterization of the Interaction between the Matrix Protein of Vesicular Stomatitis Virus and the Immunoproteasome Subunit LMP2.Inhibition and deficiency of the immunoproteasome subunit LMP7 attenuates LCMV-induced meningitis.Immunoproteasomes edit tumors, which then escapes immune recognition Human Tumor Antigens and Cancer Immunotherapy.Differential intra-proteasome interactions involving standard and immunosubunits.Three immunoproteasome-associated subunits cooperatively generate a cytotoxic T-lymphocyte epitope of Epstein-Barr virus LMP2A by overcoming specific structures resistant to epitope liberation.The immunoproteasome subunit LMP7 is required in the murine thymus for filling up a hole in the T cell repertoire.Amelioration of autoimmunity with an inhibitor selectively targeting all active centres of the immunoproteasome.Defective immuno- and thymoproteasome assembly causes severe immunodeficiency.Immunoproteasome Inhibition Impairs T and B Cell Activation by Restraining ERK Signaling and Proteostasis

P2860

Q21133685-CCF09B64-86FE-40F8-859E-0C146C7CC714 Q24337054-ECBD74B4-9AB9-4C18-8C3D-DD80223331C5 Q27024527-E2B08334-C177-4DBF-ADE8-E9801C9FDCE6 Q27693890-ADFA3A2D-F712-4501-9021-E4C339A493C7 Q27694656-AAB6DA59-E48A-4181-AD12-D4FE9988F670 Q28245575-B5BB29DA-24F3-45B6-8B79-7F29AF0D9FD1 Q33335355-5A4D0A7D-03EA-4887-94D5-7DBCC727BDFF Q34015431-FB67F369-5595-477A-B412-D99474FDACDA Q34018605-1D5639F6-98A4-4907-8BDE-79CB2A7B9797 Q34276719-637DF969-660A-4B07-B3C1-B55AB6DC33B6 Q35555565-FDF2F071-A4F6-4BAD-977D-A2E6DCA10C0D Q35834082-5ADED967-7D3D-4E44-A8FC-51166C8EEDBD Q36201122-5C7E7E78-590E-4A05-860E-C30C0A750681 Q36260235-3FA7DB9E-77B5-402C-AAA7-8EDE4DCF0AAF Q36472495-D5CE9F96-180F-4D97-98D6-50FE5BFA16D0 Q36483688-23F72AEA-1B9E-4EA1-ADD0-8365CE3AF8E4 Q36666357-E82C221F-1239-44E0-9AFE-F73DB4E7BAD1 Q37136304-2487FB0B-56B0-49D5-AC58-049CDC95DC9D Q37146941-7CDD5F37-97D4-47F1-B3A7-5F848067EFD5 Q37864471-060DFBD3-632C-436B-89AC-43657D35E724 Q38090856-F5513C75-E325-4930-A0B0-C4DCD61AAA1F Q38269935-FDB2623C-5ACE-4B45-9E31-AAC0C676B35F Q38712612-D807D58D-0E8D-4529-9E5B-012D92821FA4 Q38833090-2711B896-F6C2-407E-9465-A37A72E9E7F4 Q39352782-2D674B90-DBA1-4431-B06F-4D97F3CC9835 Q39584224-CFC10779-7EBC-44AB-8154-5B2631CC2D35 Q40140606-D57B7859-0176-4F86-A417-24BB66DFE9FF Q40602889-2FCE3223-C360-4F6E-8421-36FC41CD379F Q40954034-10046829-CAA8-4D6C-9823-89CA69AB67F5 Q41497500-587B8035-E5CA-47F6-927E-DBA8A9413B70 Q41533232-AFE92FBE-BBBE-40EF-9037-AC7FE81FEB63 Q43129632-6DFA5313-64E1-419E-BA34-D6A878F36526 Q43181859-DDE67E13-F51A-42D6-B0BA-8C66B74952FF Q47601349-D15C148E-A549-4561-A3B8-FD9FF8744E49 Q48184671-F0BD4966-1E1E-4234-A60C-3127422772BB Q52321810-F103BB06-50FD-4BE9-BECB-3AC9D56FA2C4 Q58707846-3FE7D04B-E40E-48CA-AC72-2A5D4A3B8369

P2860

Beta 2 subunit propeptides influence cooperative proteasome assembly.

http://www.wikidata.org/entity/Q34161423

description

2002 nî lūn-bûn

@nan

2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Beta 2 subunit propeptides influence cooperative proteasome assembly.

@ast

Beta 2 subunit propeptides influence cooperative proteasome assembly.

@en

Beta 2 subunit propeptides influence cooperative proteasome assembly.

@nl

type

label

Beta 2 subunit propeptides influence cooperative proteasome assembly.

@ast

Beta 2 subunit propeptides influence cooperative proteasome assembly.

@en

Beta 2 subunit propeptides influence cooperative proteasome assembly.

@nl

prefLabel

Beta 2 subunit propeptides influence cooperative proteasome assembly.

@ast

Beta 2 subunit propeptides influence cooperative proteasome assembly.

@en

Beta 2 subunit propeptides influence cooperative proteasome assembly.

@nl

P1433

Q34161423-8A881BEC-4564-4DD0-ADC3-8F4A27C548FE

P1476

Q34161423-E3B1AEF1-1CDD-40D5-8121-3557E65B3A8D

P2093

Q34161423-06FDED6A-869E-4B59-9992-EBF3AB996D3E

Q34161423-2F3FA7AD-2743-4230-82D3-4ECAD80CA176

Q34161423-4DA66079-7369-443B-8713-FF79E4398A7D

Q34161423-C379DF24-F1F6-4201-BEF5-C633A93C56C3

Q34161423-C8C245A1-9E54-44D0-AD2C-53E51F56D1D0

Q34161423-E727D55C-3FEF-4050-9421-BE9CCB7C57C5

P2860

Q34161423-0253D04F-C398-4253-9977-856858758051

Q34161423-09DF61AB-08FB-463D-A031-0E273B76D0D7

Q34161423-09F83DBB-C50A-4517-8A37-3F872CE09D89

Q34161423-2F828230-5F61-48EC-95F9-F7F03C5B6785

Q34161423-365A1D2B-8A9E-4E95-9064-8A7C0DB0545B

Q34161423-38F78B55-E919-4E58-87DF-3F8ED0EC1A0E

Q34161423-3CD35B57-4121-4B6B-ABF0-8C42BAC9AA24

Q34161423-3E0D4721-2246-4256-992E-15738531B912

Q34161423-46CA3ECB-8164-46C5-B2E7-025FB91070BE

Q34161423-4A0F5625-0BCE-4D06-8861-EB3525C0DF74

P304

Q34161423-9A644A09-7A44-4F7F-9E18-0B809C3C965F

P31

Q34161423-7AAFCA4C-DD72-4424-9111-8A715D0C8BCB

P356

Q34161423-75353C2D-2624-4DFC-820B-27E796CD8A35

P407

Q34161423-69C2CE12-A817-42FD-9990-7C26A92033EC

P433

Q34161423-6D24B176-0F86-442F-BB53-E9912FECFF9E

P478

Q34161423-75F52BCE-B573-4F5A-8FA5-D35DDC19D33A

P577

Q34161423-05E64EF6-EB5F-4934-A213-4267D861C36E

P698

Q34161423-14F28204-6A8D-4072-9F25-1760559639F2

P356

P1433

Journal of Biological Chemistry

P1476

Beta 2 subunit propeptides influence cooperative proteasome assembly.

@en

P2093

John J Monaco

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

Krupakar Jayarapu

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

Laura Elenich

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

Mita De

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

Robert A Colbert

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

Thomas A Griffin

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

P2860

Subunit arrangement in the human 20S proteasome

Structure and functions of the 20S and 26S proteasomes

Structure of 20S proteasome from yeast at 2.4 A resolution

Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly.

Identical subunit topographies of human and yeast 20S proteasomes

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

A protein catalytic framework with an N-terminal nucleophile is capable of self-activation

In vivo assembly of the proteasomal complexes, implications for antigen processing

The proteasome: paradigm of a self-compartmentalizing protease

Degradation of cell proteins and the generation of MHC class I-presented peptides.

P304

6153-6159

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

P31

scholarly article

P356

10.1074/JBC.M209292200

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

P407

P433

8

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

P478

278

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

P577

2002-11-26T00:00:00Z

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

P698

12456675

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