Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability - Test2 - elhamkhani - TriplyDB

Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability

Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability

http://www.wikidata.org/entity/Q26829490

about

The importance of ribosome production, and the 5S RNP-MDM2 pathway, in health and disease Pathways to Specialized Ribosomes: The Brussels Lecture Nuclear PI3K signaling in cell growth and tumorigenesis New insights into nucleolar structure and function Structure of human MDM2 complexed with RPL11 reveals the molecular basis of p53 activation Inhibition of RNA polymerase I transcription initiation by CX-5461 activates non-canonical ATM/ATR signaling Ribosomal protein L23 negatively regulates cellular apoptosis via the RPL23/Miz-1/c-Myc circuit in higher-risk myelodysplastic syndrome Whole-genome RNAi screen highlights components of the endoplasmic reticulum/Golgi as a source of resistance to immunotoxin-mediated cytotoxicity Stabilization of SIRT7 deacetylase by viral oncoprotein HBx leads to inhibition of growth restrictive RPS7 gene and facilitates cellular transformation.Crude Extracts, Flavokawain B and Alpinetin Compounds from the Rhizome of Alpinia mutica Induce Cell Death via UCK2 Enzyme Inhibition and in Turn Reduce 18S rRNA Biosynthesis in HT-29 Cells.Regulation of the MDM2-p53 pathway by the nucleolar protein CSIG in response to nucleolar stress.Neuronal GPCR OCTR-1 regulates innate immunity by controlling protein synthesis in Caenorhabditis elegans.Role of the nucleus in apoptosis: signaling and execution.Disruption of the RP-MDM2-p53 pathway accelerates APC loss-induced colorectal tumorigenesis.RP-MDM2-p53 Pathway: Linking Ribosomal Biogenesis and Tumor Surveillance.Ribosomopathy-like properties of murine and human cancers.Modulation of the p53 family network by RNA-binding proteins.Protection against High-Fat-Diet-Induced Obesity in MDM2C305F Mice Due to Reduced p53 Activity and Enhanced Energy Expenditure.A ribosomal protein AgRPS3aE from halophilic Aspergillus glaucus confers salt tolerance in heterologous organisms.Down-regulation of RPS9 Inhibits Osteosarcoma Cell Growth through Inactivation of MAPK Signaling Pathway Farnesiferol c induces apoptosis via regulation of L11 and c-Myc with combinational potential with anticancer drugs in non-small-cell lung cancers.HT-SuperSAGE of the gut tissue of a Vip3Aa-resistant Heliothis virescens (Lepidoptera: Noctuidae) strain provides insights into the basis of resistance.Ribosomal protein L4 is a novel regulator of the MDM2-p53 loop.Expression and RNA Interference of Ribosomal Protein L5 Gene in Nilaparvata lugens (Hemiptera: Delphacidae).SinEx DB: a database for single exon coding sequences in mammalian genomes.RNA-Seq of Human Neural Progenitor Cells Exposed to Lead (Pb) Reveals Transcriptome Dynamics, Splicing Alterations and Disease Risk Associations.Ribosomal stress and Tp53-mediated neuronal apoptosis in response to capsid protein of the Zika virus.RPL23 Links Oncogenic RAS Signaling to p53-Mediated Tumor Suppression.Pre-45s rRNA promotes colon cancer and is associated with poor survival of CRC patients.Molecular characterization of AmiC, a positive regulator in acetamidase operon of Mycobacterium smegmatis.The GAIT translational control system.Involvement of RPL11 in the enhancement of P53 stability by a podophyllum derivative, a topoisomerase II inhibitor.How Ribosomes Translate Cancer.Inactivation of ribosomal protein S27-like confers radiosensitivity via the Mdm2-p53 and Mdm2-MRN-ATM axes.Transfer of Allogeneic CD4+ T Cells Rescues CD8+ T Cells in Anti-PD-L1-Resistant Tumors Leading to Tumor Eradication.BCCIPβ modulates the ribosomal and extraribosomal function of S7 through a direct interaction.Proapoptotic Requirement of Ribosomal Protein L11 in Ribosomal Stress-Challenged Cortical Neurons.hnRNP R and its main interactor, the noncoding RNA 7SK, coregulate the axonal transcriptome of motoneurons.SPIN1 promotes tumorigenesis by blocking the uL18 (universal large ribosomal subunit protein 18)-MDM2-p53 pathway in human cancer.Localization of RNA and translation in the mammalian oocyte and embryo.

P2860

Q26741340-C3142CBF-2825-4695-BCBD-7F65591EA726 Q26772082-E03FF6EA-BA66-409D-84AC-2060390530B9 Q26859127-3A6E6552-DBEA-409E-9A29-BA3D244FF345 Q27015674-D41B8E16-E7BF-42F4-A6C2-7E717AC1980D Q27322960-47D43BB1-14E2-4C06-BDE8-9A88F371C16F Q28468631-BBC1237D-40F3-4641-AFB9-7795F2B986B6 Q33725731-BFE84BB4-DD85-4B6C-9E72-9509A000668D Q35189855-C12E06F7-95DC-49CF-B002-D7E648AB348F Q36129012-2A255EC1-B91B-4E12-98DC-3BBC71709AE7 Q36254067-CCEC4136-2C7A-4B54-BC3C-79E868744FBE Q37394276-37446C8D-7793-434A-BB58-92CEB3A6395D Q37408322-F107D425-0DEE-4124-93EE-989D935AA175 Q38582491-2D582FAE-2B2D-4F38-AAD0-BF0D706A4F1E Q39401623-888B0F45-9FEA-48A3-8135-088C95D8A793 Q39456968-AEA31110-72C2-45B5-96D9-547A3D18D6B5 Q40078177-E4015065-48C0-4938-8543-2665AFC1D509 Q41277033-5C15038A-F3F9-4CF2-ABC6-5A55B84842BB Q41443354-1BF4FC25-F6B1-440C-B521-249363F79412 Q41493915-8FD42E71-1DE0-4864-87E8-D90D4988D1E6 Q41721808-2923970F-F376-4B5C-A706-80C80CB48B48 Q41825963-CBB9707C-2BED-4BB8-AB56-73D820419B28 Q41986029-1D4FFB49-3E5D-45A7-AEF7-2801D05942C9 Q42065038-B2527815-794B-4B5C-8836-476E27EF778D Q42102028-07F6CD48-47BF-4C32-92FA-EE87A7387BFC Q42737905-F57E977A-CD96-4BBD-9817-B3DA5258D46F Q42777677-B8B3A977-C62A-4436-A09C-F311C97A64D3 Q45323962-1023CD91-7354-460C-9F79-6BFCF4191B21 Q46898426-B1558103-BAC8-4C46-91B5-3088839A9604 Q47160718-FA425A9C-C651-41C7-BCB3-F91FCA28ACA9 Q47259188-26B7F6DC-24C9-4590-BA61-87D1807F4CEA Q47387876-4D7CFE93-53B8-4936-9E08-180D92EC046C Q47742463-E660D415-FD29-4EC3-96E1-A177C6C218A8 Q47782255-6BB6FB47-874F-4140-AB03-B45D0F889A7E Q49358552-19DF23F3-0BB2-4BF0-981A-D07F20135344 Q50957786-9BFEFBB8-1F81-4247-ABF5-8C14752E79FD Q50998094-64C28CCE-F5A0-4EFF-9742-5A826A3E0256 Q51263731-592ACDA4-ABFC-4161-AE90-29BD77F6C799 Q52366535-9E75888A-744E-42EA-9BF2-0492A420D6D8 Q52652467-BEEB9629-72B0-4F56-9DFE-22115DF16269 Q55250563-DE51D5B1-A328-4718-A964-87AE405768BE

P2860

Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability

http://www.wikidata.org/entity/Q26829490

description

2014 nî lūn-bûn

@nan

2014 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability

@ast

Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability

@en

Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability

@nl

type

label

Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability

@ast

Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability

@en

Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability

@nl

prefLabel

Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability

@ast

Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability

@en

Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability

@nl

P1433

Q26829490-FC24E3BE-4B46-4F0C-AE34-2DF27FAE8A8A

P1476

Q26829490-2BA92A4E-337D-4307-A033-1ACF84DB2E1E

P2093

Q26829490-091478EA-4473-47BA-A03D-2531600D3E8B

Q26829490-237E2259-A9FB-47F2-A3C0-4FF066B08207

Q26829490-A74375B3-0A16-4898-8692-9144575B05B6

P275

Q26829490-A942FA83-3837-4D5F-A271-D7749BA07CA3

P2860

Q26829490-022CA020-86A2-4AB0-AB22-17BA41967B61

Q26829490-029C226A-B61A-4EC5-9BCB-145327D76DAD

Q26829490-03FC3301-80E9-4062-A102-CEF7C79328C6

Q26829490-04A07E3F-E76D-4838-B62A-4A220BA0DDC8

Q26829490-04EBBD49-8A11-482E-AB9E-2B59945885CD

Q26829490-05AB1282-30D1-495E-8D3A-E6C9283E80AF

Q26829490-06CD6342-7048-4C2A-A2D3-5808E987B31D

Q26829490-09825F36-BA5C-468A-95EE-08709BD5E777

Q26829490-0EAAEC01-9CE0-4D03-86A6-7D0F158023AF

Q26829490-0FCA90F8-543A-4155-B742-C20B8BF282FD

P304

Q26829490-F7AC059E-C872-4EDF-8847-8AE91978B5FF

P31

Q26829490-6A6FB111-EFA6-48A7-852A-EF6E1A427E7B

Q26829490-BD13ECC9-092A-4C2B-8D92-AF5C79970D93

P3181

Q26829490-EFC96B7C-8C29-4184-BD5C-9E62B609F850

P356

Q26829490-2A7A04BF-6E35-48C7-AE3F-25377A4675E5

P407

Q26829490-5FC72768-7571-4310-84C5-90C27BDBA5A2

P433

Q26829490-DE8622C4-83F4-4076-9600-7CAFEBEA178F

P478

Q26829490-9989D733-1D0B-469D-AB30-71E2225CCB9B

P577

Q26829490-FA277CB3-FFBC-4CDD-85B5-BB907B579902

P5875

Q26829490-7AD12FF8-B9BA-4C6F-ACA0-D2F9D90294C9

P698

Q26829490-44B2936E-0AAC-4747-82C4-4A8A5C611E77

P921

Q26829490-080B6438-C436-4ACA-A215-2970E1E35657

Q26829490-11034E39-F0B5-40F7-8A5B-197087DC9CE4

Q26829490-2E473338-E8DF-49DE-9011-2CFA3922E4D5

Q26829490-4D455D40-6053-42AB-A66E-79502F7B4A2E

Q26829490-4E4A99A4-9A85-482D-84AB-A6A6A95782B4

Q26829490-5276417C-6B7A-4DBD-AA02-76ED8C1CBEC4

Q26829490-6C3C3342-639A-4819-88D2-E0718BD05A3D

Q26829490-E7370825-7D82-466D-93C0-16BB1BF8DE6A

P932

Q26829490-760318F5-64DA-455A-8C83-2033853DC5C2

P3181

P356

ONCOTARGET.1784

P1433

P1476

Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability

@en

P2093

Patrick Leslie

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

Tae-Hyung Kim

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

Yanping Zhang

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

P275

Creative Commons Attribution 2.5 Unported

P2860

Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein

Human ribosomal protein S13 regulates expression of its own gene at the splicing step by a feedback mechanism

Ribosomal protein S7 as a novel modulator of p53-MDM2 interaction: binding to MDM2, stabilization of p53 protein, and activation of p53 function

HDM2-binding partners: interaction with translation elongation factor EF1alpha.

Identification of RPS14 as a 5q- syndrome gene by RNA interference screen

Regulation of human RPS14 transcription by intronic antisense RNAs and ribosomal protein S14

A map of 75 human ribosomal protein genes

MDMX regulation of p53 response to ribosomal stress

Ribosomal protein S27-like and S27 interplay with p53-MDM2 axis as a target, a substrate and a regulator

Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain

P304

860-71

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

P31

scholarly article

P3181

980710

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

P356

10.18632/ONCOTARGET.1784

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

P407

P433

4

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

P478

5

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

P577

2014-02-28T00:00:00Z

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

P5875

261033809

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

P698

24658219

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

P921

nuclear protein

DNA-binding protein

transport protein

ribosomal proteins

proto-oncogene proteins

neoplasm proteins

P932

4011588

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