RNF4-dependent hybrid SUMO-ubiquitin chains are signals for RAP80 and thereby mediate the recruitment of BRCA1 to sites of DNA damage.
about
Choreographing the Double Strand Break Response: Ubiquitin and SUMO Control of Nuclear ArchitectureHow SUMOylation Fine-Tunes the Fanconi Anemia DNA Repair PathwayCooperativity of the SUMO and Ubiquitin Pathways in Genome StabilityRole of Deubiquitinating Enzymes in DNA RepairRPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage responseCrosstalk between ubiquitin and other post-translational modifications on chromatin during double-strand break repairMultivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMOSUMO-mediated regulation of DNA damage repair and responsesUbiquitylation, neddylation and the DNA damage responseUSP45 deubiquitylase controls ERCC1-XPF endonuclease-mediated DNA damage responsesMolecular Characterization and Functional Analysis of Annulate Lamellae Pore Complexes in Nuclear Transport in Mammalian Cells.SUMOylation of ATRIP potentiates DNA damage signaling by boosting multiple protein interactions in the ATR pathwayUSP13 regulates the RAP80-BRCA1 complex dependent DNA damage response.The role of ubiquitination and sumoylation in diabetic nephropathy.Exploring the RING-catalyzed ubiquitin transfer mechanism by MD and QM/MM calculations.An arginine-rich motif of ring finger protein 4 (RNF4) oversees the recruitment and degradation of the phosphorylated and SUMOylated Krüppel-associated box domain-associated protein 1 (KAP1)/TRIM28 protein during genotoxic stress.Intrinsic disorder drives N-terminal ubiquitination by Ube2wNoncovalent interactions with SUMO and ubiquitin orchestrate distinct functions of the SLX4 complex in genome maintenance.BLM SUMOylation regulates ssDNA accumulation at stalled replication forks.Deciphering the BRCA1 Tumor Suppressor Network.Identification of RNF168 as a PML nuclear body regulatorMERIT40 cooperates with BRCA2 to resolve DNA interstrand cross-links.Ubiquitin-H2AX fusions render 53BP1 recruitment to DNA damage sites independent of RNF8 or RNF168Heterochromatic breaks move to the nuclear periphery to continue recombinational repair.SUMO-targeted ubiquitin ligase activity can either suppress or promote genome instability, depending on the nature of the DNA lesion.Sequential posttranslational modifications regulate PKC degradation.RNF4 regulates DNA double-strand break repair in a cell cycle-dependent mannerGenetic evaluation of BRCA1 associated a complex genes with triple-negative breast cancer susceptibility in Chinese women.Structural mechanisms underlying signaling in the cellular response to DNA double strand breaks.A SUMO-targeted ubiquitin ligase is involved in the degradation of the nuclear pool of the SUMO E3 ligase Siz1.DNA damage emergency: cellular garbage disposal to the rescue?Decoding the SUMO signal.Reading, writing, and repair: the role of ubiquitin and the ubiquitin-like proteins in DNA damage signaling and repair.The SUMO system: a master organizer of nuclear protein assemblies.SUMO rules: regulatory concepts and their implication in neurologic functions.RNA splicing: a new player in the DNA damage responseSpatiotemporal regulation of posttranslational modifications in the DNA damage response.Total chemical synthesis of SUMO-2-Lys63-linked diubiquitin hybrid chains assisted by removable solubilizing tags.A high-yield double-purification proteomics strategy for the identification of SUMO sites.Chemical and semisynthetic approaches to study and target deubiquitinases.
P2860
Q26744843-B769BBAB-37A4-4BE5-AA0D-41AF91D544FDQ26752451-DF408D7B-5AFC-40AF-B75A-A9F42E8B5656Q26765420-486C3481-DDC9-4B09-83A6-58DA4B7A4A05Q26773800-41FFB12A-5F2A-4AD3-A0FF-48D74B3895A8Q26827954-7D1A7F6E-5F0E-429E-928D-E5DE283A64DFQ27023465-F8DC7F68-CDA5-4ABA-B162-F55CDD6F32F1Q27680434-2BE41948-D695-4EEF-8919-6B64FE3B0593Q28086764-2BF35BCE-6B23-4E30-9D0B-2C314EADDE3EQ28087342-48FC10B1-984F-4235-876E-633F2AEFBD86Q28115910-E25F8C88-9BEA-4515-8659-8CB9F95B4EE0Q30362076-09F24CCB-10E7-403F-9FE9-B1D2DF367FEBQ31171264-96EB9CB3-32A8-492E-9449-63C5507FEEE1Q33770883-6D40E1E6-3CAB-4849-911D-3A899FCDB69EQ33786922-69B1CEDC-0E22-40A5-959D-08C961A3FE2EQ33864109-54E525BC-E396-4E28-8DF3-75380966D180Q33947105-910F4F62-28E2-46A9-8A1D-4FB00D459C26Q34450191-DFA98D2B-53BC-4AD9-A9F3-4A0AE14692B4Q34898909-8619B294-2C52-441E-9062-6E7FA537B9EBQ34985577-E1B9043C-73A0-4096-AAEE-801852496DFCQ35859458-F8058A0D-B6D4-422F-B8D0-339D096422F4Q35870845-9D81F542-0236-4C9A-824F-F58037A30071Q36084327-F7B7F45D-D611-46F5-B354-67507C369D8CQ36189465-7F0BF121-6EF9-465E-B5AA-0A1ED811C256Q36235927-E4418A36-1D58-4114-86FB-24F3C0741AEBQ36364249-6474FD12-1102-4486-B846-DD61FF7F52A1Q36463365-631FA6C3-AD84-40D1-8056-B32DBD7E0C46Q36838400-3FFAF5F4-2935-4396-9E6D-828495906E07Q36962780-7D135F2E-01FE-41E9-AAEE-D2F8B7949727Q37282157-8A40F778-DAF5-4B85-B9FE-40F5EAA2CCBEQ37416477-0C870A4E-7E2F-4CE3-A826-1E5F4AF1657FQ38090434-94882853-9CC7-43C1-AE21-9B08CA998DBEQ38091465-944785A9-414E-417F-8B9B-597586973DC6Q38095917-55EA7A54-03F1-4515-8A15-A78459417339Q38126813-7DD78133-B86A-4F13-8380-E05949D769E6Q38132691-5E7F5F0F-65B4-4A60-89B2-8E0292CF2263Q38155497-A532F850-3866-44AF-B7B4-3D9481A14F37Q38656328-18E71EA0-B776-4111-A933-77CC1127908BQ38674907-E9EA71A0-F159-4A89-89E9-7A330C23A5AFQ38750217-A3097A62-9C8F-4433-B567-66013240B3A1Q38799376-355050E1-D7CA-41D4-AA97-D565111F68C0
P2860
RNF4-dependent hybrid SUMO-ubiquitin chains are signals for RAP80 and thereby mediate the recruitment of BRCA1 to sites of DNA damage.
description
2012 nî lūn-bûn
@nan
2012 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
RNF4-dependent hybrid SUMO-ubi ...... BRCA1 to sites of DNA damage.
@ast
RNF4-dependent hybrid SUMO-ubi ...... BRCA1 to sites of DNA damage.
@en
RNF4-dependent hybrid SUMO-ubi ...... BRCA1 to sites of DNA damage.
@nl
type
label
RNF4-dependent hybrid SUMO-ubi ...... BRCA1 to sites of DNA damage.
@ast
RNF4-dependent hybrid SUMO-ubi ...... BRCA1 to sites of DNA damage.
@en
RNF4-dependent hybrid SUMO-ubi ...... BRCA1 to sites of DNA damage.
@nl
prefLabel
RNF4-dependent hybrid SUMO-ubi ...... BRCA1 to sites of DNA damage.
@ast
RNF4-dependent hybrid SUMO-ubi ...... BRCA1 to sites of DNA damage.
@en
RNF4-dependent hybrid SUMO-ubi ...... BRCA1 to sites of DNA damage.
@nl
P2093
P2860
P50
P1433
P1476
RNF4-dependent hybrid SUMO-ubi ...... f BRCA1 to sites of DNA damage
@en
P2093
Ajit Datta
Catherine M Guzzo
Roger A Greenberg
Vibhor Gupta
P2860
P356
10.1126/SCISIGNAL.2003485
P577
2012-12-04T00:00:00Z