Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants. - Wikidata - wikimedia - TriplyDB

Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants.

Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants.

http://www.wikidata.org/entity/Q34753108

about

Hepatitis C virus non-structural protein NS3 interacts with LMP7, a component of the immunoproteasome, and affects its proteasome activity The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its death Cross Talk of Proteostasis and Mitostasis in Cellular Homeodynamics, Ageing, and Disease MHC class I antigen processing and presenting machinery: organization, function, and defects in tumor cells One-shot NMR analysis of microbial secretions identifies highly potent proteasome inhibitor The 19 s proteasome subcomplex establishes a specific protein interaction network at the promoter for stimulated transcriptional initiation in vivo.The ubiquitin-proteasome pathway and proteasome inhibitors The origin of proteasome-inhibitor resistant HLA class I peptidomes: a study with HLA-A*68:01 Proteasome proteolysis supports stimulated platelet function and thrombosis Computational prediction of cleavage using proteasomal in vitro digestion and MHC I ligand data.Discrete cleavage motifs of constitutive and immunoproteasomes revealed by quantitative analysis of cleavage products.Why does threonine, and not serine, function as the active site nucleophile in proteasomes?Global analysis of proteasomal substrate specificity using positional-scanning libraries of covalent inhibitors.Cleavage motifs of the yeast 20S proteasome beta subunits deduced from digests of enolase 1.The caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites.Proteasomal chymotrypsin-like peptidase activity is required for essential functions of human monocyte-derived dendritic cells.Role of proteasomes in disease.Proteasome inhibition suppresses essential immune functions of human CD4+ T cells.Genetic analyses of the Arabidopsis 26S proteasome regulatory particle reveal its importance during light stress and a specific role for the N-terminus of RPT2 in development Aging is not associated with proteasome impairment in UPS reporter mice.Double positive CD4CD8 alphabeta T cells: a new tumor-reactive population in human melanomas Colorectal cancer and NF-κB signaling pathway The proteasome activator 11 S REG (PA28) and class I antigen presentation The specificity of proteasomes: impact on MHC class I processing and presentation of antigens.Proteolysis and class I major histocompatibility complex antigen presentation.Human T-cell leukemia virus type 1 Tax protein binds to assembled nuclear proteasomes and enhances their proteolytic activity.How an inhibitor of the HIV-I protease modulates proteasome activity.Proteasome inhibitors: from in vitro uses to clinical trials.Discovery of a potent and highly β1 specific proteasome inhibitor from a focused library of urea-containing peptide vinyl sulfones and peptide epoxyketones.Two abundant proteasome subtypes that uniquely process some antigens presented by HLA class I molecules.The proteasome system in infection: impact of β5 and LMP7 on composition, maturation and quantity of active proteasome complexes Nature of pharmacophore influences active site specificity of proteasome inhibitors.Comprehensive quantitative analysis of ovarian and breast cancer tumor peptidomes.Proteolytic pathways induced by herbicides that inhibit amino acid biosynthesis.Mechanisms of MHC class I-restricted antigen presentation.Posttranslational modification and cell type-specific degradation of varicella-zoster virus ORF29p.Trypanosoma cruzi infection down-modulates the immunoproteasome biosynthesis and the MHC class I cell surface expression in HeLa cells.Disruption of protein quality control in Parkinson's disease.Molecular machines for protein degradation.Inhibition of Proteasome Activity by Low-dose Bortezomib Attenuates Angiotensin II-induced Abdominal Aortic Aneurysm in Apo E(-/-) Mice.

P2860

Q24300867-4B7A1C81-DE1E-4F80-A1DC-5D8ACE0DAD50 Q26738549-2EE08FC6-5E40-4CB8-900A-B284B1FB39B4 Q26765684-EB6F9E70-680A-49C2-9748-35A3D3597421 Q26866479-5D998F0E-A7EA-401F-A3D9-699C5E67BB0F Q27674685-41F5739E-5721-4850-ADA1-61FBB0DD392E Q27929848-F4C7D36C-65C6-41B2-8081-E794732DB92F Q28367002-77BC26E3-4215-462E-B744-847500F1F09E Q30423203-96A58573-7A3E-42B9-A631-8C0E909DC75E Q30580785-623A1CD7-9E35-4D82-B440-E1A9BEE99E34 Q30665275-F9FDBF1E-E751-4F29-B19A-A14DACF0A9B5 Q30685494-82329750-503E-4485-8202-1D0A3588E929 Q30870481-1FF50827-9400-4AC1-A150-91794B23BBA6 Q30983359-CA9C29A2-73F1-44B5-BDD2-A354A9C258C9 Q32000515-5D5907F3-B97B-4617-B0FD-88F5CC960991 Q33187465-7B0B966F-E23D-43A5-A567-455376E0BFA0 Q33262643-945BAA81-6267-4B43-9066-F8C0359CBBAC Q33307877-D7FE52CD-0104-4D41-B1F9-7588B33DF15D Q33316357-DD6635BB-3EBD-4CD2-A43A-6009E3D6B4B0 Q33354004-65862C1B-5D3F-44F6-9988-CAF221E7AC43 Q33466066-622F5780-9EF5-4EE8-9522-778C5CDCF112 Q33522240-507E5094-07C2-4693-AE24-5875A5BE2A0E Q33596306-745AF402-7EE7-453C-81AD-C9EAF27A47CD Q33796158-B7339FE6-F931-42AC-AD0D-810A4BB2519F Q33815363-D1CC59E4-89E0-4A73-A563-CA3961CE0A15 Q33815369-E0BB13BE-272F-4F9C-91F3-80B36D1A7CE5 Q33849258-338C68F3-3746-458D-8EB7-0070B656A0CF Q33882609-31B0426C-FB8F-4246-BCDE-8BB062479390 Q34052405-21604327-2F48-403B-9393-E38AD9F995E5 Q34079904-78DF30EE-CF3C-4066-97E0-3ACC36ABA96A Q34276719-9DF6DBC1-FCA6-4556-9976-C625B10A7177 Q34328313-250D9997-E7F5-4C9C-8D03-42982A8655A7 Q34401062-19A23036-3726-45E6-B906-10089431FF49 Q34855337-E964CB39-4B84-4A00-B2C5-83F019878311 Q34989409-225B3DFA-9916-4DA7-8120-5B28DBBBE1A1 Q35050403-9600D59A-091F-4DC4-AC91-F71DEE96E173 Q35139289-D8413ACB-C508-429A-AC37-4F0B9F31BD8D Q35154144-FB0CD112-D43F-4A73-880C-53C9E556E402 Q35902695-4A907054-6984-4743-875F-9DA87EAFFE95 Q36023030-0EA10140-ACCF-49AE-BB0B-82398994D255 Q36217025-CA52B9E8-C3E5-4DDE-8377-511CE2752425

P2860

Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants.

http://www.wikidata.org/entity/Q34753108

description

1998 nî lūn-bûn

@nan

1998 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

1998年の論文

@ja

1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

name

Contribution of proteasomal be ...... s analyzed with yeast mutants.

@ast

Contribution of proteasomal be ...... s analyzed with yeast mutants.

@en

Contribution of proteasomal be ...... s analyzed with yeast mutants.

@nl

type

label

Contribution of proteasomal be ...... s analyzed with yeast mutants.

@ast

Contribution of proteasomal be ...... s analyzed with yeast mutants.

@en

Contribution of proteasomal be ...... s analyzed with yeast mutants.

@nl

prefLabel

Contribution of proteasomal be ...... s analyzed with yeast mutants.

@ast

Contribution of proteasomal be ...... s analyzed with yeast mutants.

@en

Contribution of proteasomal be ...... s analyzed with yeast mutants.

@nl

P1433

Q34753108-8B71A723-294F-4F03-872A-FB5C2ADE35F3

P1476

Q34753108-77B6D954-28D6-477B-8FE5-02D9C43122CD

P2093

Q34753108-13F4F211-08D5-4F52-9F6A-DB0D7BF131DC

Q34753108-184821B5-5B77-4DE0-947F-44E45EE55022

Q34753108-691202CF-051E-4590-AEE2-7F09478116F6

Q34753108-6B7904ED-499D-4A4F-B519-74EDF558AFDF

Q34753108-87A7C9B2-6EBC-4932-B21A-1897E4F1BEC3

Q34753108-BF1F16EE-7118-4CC3-A700-EA03EAE0F5A4

Q34753108-C5EF1FD5-72B4-4E83-8440-5EED916E0B19

Q34753108-CD427A4E-3BC3-4ECC-9E06-C7DBC7CCB5CD

Q34753108-CEC3661D-99AB-4CA3-9849-1F27A1471049

Q34753108-E2DF5B54-1DD6-49D2-A243-59C6328AF4AB

P2860

Q34753108-0B50FD13-D615-42D1-B2E5-CB3C7044E7C0

Q34753108-1AF497E0-823C-4B42-BE20-9007961AA6D5

Q34753108-1FBEBBC4-CFB3-461D-87AA-E50110124100

Q34753108-29D4A610-FBFD-4322-8C1A-E62DB27C8637

Q34753108-37C6DB4E-33CF-4E51-90F6-99A7EEE2C242

Q34753108-46693286-BC8D-491C-8059-69CC7E1C87A1

Q34753108-480E29F9-060C-4871-A336-B5A9B8199F20

Q34753108-4B3C59BB-8079-4A9A-B6B8-580E526FD81C

Q34753108-4E73626B-0F11-4335-94AA-DF7FE2F68375

Q34753108-598FECD7-81A8-46EA-B530-8C0FBD5116A8

P304

Q34753108-3E977DF0-2828-48B5-A671-DB1FEA08D986

P31

Q34753108-55A2CE4F-B5D1-4720-90E7-C89D70755825

P356

Q34753108-17874B1C-96F4-4F11-AC9E-8D3541A81AC3

P407

Q34753108-361B9609-4125-4776-97EE-49801C5C9830

P433

Q34753108-FF2B4EAB-62AB-4FF4-B333-36A1F82233B7

P478

Q34753108-9699F56F-E358-4BEC-BD04-72C0220A1F5F

P577

Q34753108-7058A46D-A185-4228-BE93-7EF9660A9DA9

P5875

Q34753108-7A0BF497-06AF-4ED1-8B71-CE8658CED5CB

P698

Q34753108-00230EBF-00E1-4A05-9D77-2E81BEF0AB04

P356

JBC.273.40.25637

P1433

Journal of Biological Chemistry

P1476

Contribution of proteasomal be ...... s analyzed with yeast mutants.

@en

P2093

Deeg M

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

Dick TP

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

Groll M

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

Heinemeyer W

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

Huber R

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

Keilholz W

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

Nussbaum AK

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

Rammensee HG

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

Schild H

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

Schirle M

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

P2860

Subunit arrangement in the human 20S proteasome

Newly identified pair of proteasomal subunits regulated reciprocally by interferon gamma

Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction

Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution

Structure of 20S proteasome from yeast at 2.4 A resolution

ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway.

Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation.

The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing.

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

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

P304

25637-25646

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

P31

scholarly article

P356

10.1074/JBC.273.40.25637

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

P407

P433

40

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

P478

273

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

P577

1998-10-01T00:00:00Z

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

P5875

13538142

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

P698

9748229

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