about
Histone H4 lysine 20 monomethylation promotes transcriptional repression by L3MBTL1Replication-Associated Recombinational Repair: Lessons from Budding YeastFunctions and regulation of the multitasking FANCM family of DNA motor proteinsStructural and Functional Insights into the Roles of the Mms21 Subunit of the Smc5/6 ComplexBinding of the Fkh1 Forkhead Associated Domain to a Phosphopeptide within the Mph1 DNA Helicase Regulates Mating-Type Switching in Budding Yeast.Ubc9- and mms21-mediated sumoylation counteracts recombinogenic events at damaged replication forks.Smc5-Smc6 mediate DNA double-strand-break repair by promoting sister-chromatid recombination.Interplay between the Smc5/6 complex and the Mph1 helicase in recombinational repairNucleoporins prevent DNA damage accumulation by modulating Ulp1-dependent sumoylation processesSUMO-mediated regulation of DNA damage repair and responsesCooperation of sumoylated chromosomal proteins in rDNA maintenanceRegulation of Ku-DNA association by Yku70 C-terminal tail and SUMO modificationSumoylation of the Rad1 nuclease promotes DNA repair and regulates its DNA associationThe Smc5/6 complex and Esc2 influence multiple replication-associated recombination processes in Saccharomyces cerevisiaeRad52 SUMOylation affects the efficiency of the DNA repair.The Smc5-Smc6 complex regulates recombination at centromeric regions and affects kinetochore protein sumoylation during normal growth.Restriction of replication fork regression activities by a conserved SMC complex.A versatile scaffold contributes to damage survival via sumoylation and nuclease interactionsConcerted and differential actions of two enzymatic domains underlie Rad5 contributions to DNA damage tolerance.Sumoylation influences DNA break repair partly by increasing the solubility of a conserved end resection protein.Selective modulation of the functions of a conserved DNA motor by a histone fold complex.DNA break-induced sumoylation is enabled by collaboration between a SUMO ligase and the ssDNA-binding complex RPA.SUMOylation regulates telomere length homeostasis by targeting Cdc13.Homologous recombination and its regulationRtt107 Is a Multi-functional Scaffold Supporting Replication Progression with Partner SUMO and Ubiquitin Ligases.Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylationA STUbL wards off telomere fusions.Differential regulation of the anti-crossover and replication fork regression activities of Mph1 by Mte1.A new MCM modification cycle regulates DNA replication initiation.Lif1 SUMOylation and its role in non-homologous end-joining.DNA damage checkpoint and recombinational repair differentially affect the replication stress tolerance of Smc6 mutants.The Rtt107 BRCT scaffold and its partner modification enzymes collaborate to promote replication.SUMOylation of Rad52-Rad59 synergistically change the outcome of mitotic recombination.Replication fork regression and its regulation.Multi-BRCT scaffolds use distinct strategies to support genome maintenance.A guide for targeted SUMO removal.Smc5/6 Mediated Sumoylation of the Sgs1-Top3-Rmi1 Complex Promotes Removal of Recombination Intermediates.Architecture of the Smc5/6 Complex of Saccharomyces cerevisiae Reveals a Unique Interaction between the Nse5-6 Subcomplex and the Hinge Regions of Smc5 and Smc6Extensive DNA damage-induced sumoylation contributes to replication and repair and acts in addition to the mec1 checkpoint.The Slx5-Slx8 complex affects sumoylation of DNA repair proteins and negatively regulates recombination.
P50
Q24320777-DD7983CF-1235-45B0-9944-9C0EE95E8985Q26739929-6C47D9E2-12D2-4739-8AE2-A7CD5DF4E5FCQ26784076-D366EDD7-F2AE-42F0-A420-28E9AE85194AQ27657416-9B9865F5-E974-4091-8044-514F3F1435F2Q27930012-DE786B1E-8B3A-4166-88F9-F5A497C9F1DFQ27930441-86F30B93-9903-4511-91F8-C20240901E0FQ27931113-CAACA4D1-FF98-433B-A3C6-B329A76AEBE4Q27933139-31A87057-30AE-4694-9280-D66EACB5B74AQ27938451-701795FD-5DE9-4764-B4F2-B8DFF3CFE5BAQ28086764-C8B5AB1C-44A6-4A6C-BF4D-1694C94F3BD6Q28473816-013A7152-3C70-4F76-BD67-81B64F9C6067Q33675631-E829A274-467A-4C62-960A-5BBF2F6B726FQ33698685-3E3CDB33-AA6F-4C14-8EF5-9292471CA351Q33948571-93CCE3F2-1E61-4FCD-9712-B17CAC0334FCQ34058338-453D112D-2B68-4747-B29D-CB0AE25F908EQ34531945-A1ADE5F6-0C13-4A8E-AD41-28C468C9B755Q34714389-20293B22-EF7E-4306-9E15-C1A111B1265DQ34792868-7E25755F-B962-4CAB-9A2A-72931741439BQ35171543-7D0086FB-9FB2-42E4-BDD0-31DCB8A3D716Q35539883-380BE9D8-DE7F-48F3-88BE-4A152822139EQ35635439-19A2FE9E-7978-4E49-BE3C-203E3FD79CE1Q35740310-4DC9D2CE-CFBD-409E-8B36-999532986936Q35794091-E632D9E7-7098-4AD4-9823-EDAF85DC3E21Q36106937-D2A8F9CB-7717-41B8-86AB-1DE9F7415623Q36172725-070FFD75-70BE-4C8D-BAF0-38DE1266907CQ36228483-2D1C6854-6677-4CFE-8DB3-3C41F54DDEA9Q36706120-5C686E25-86B4-47F8-8662-AE8F704358B9Q36715620-E35B3B74-1E79-4971-B21B-2E840E646B87Q36775152-D10C41A1-41BA-459F-A358-0BEBA8E553F5Q36878460-04E332FC-5D60-4EAE-9799-B48AF91C2327Q37056627-F67D459B-22C8-4D1A-A254-72F637D2351AQ37289716-41EC0996-3024-40C9-9614-D2D4913E52C6Q37313069-47F2FE99-0621-4B89-A0F3-A0E4394C2C7BQ38778587-822B6CC1-0535-4EC0-A112-70B8D7180BD4Q38942428-1D127AFF-06B9-4AE9-936D-CCA12E3571CCQ39312146-50B702CB-9D5D-4DA5-B17A-B34C27ACA7BAQ41335010-DE197056-6A40-4A14-B34F-1943F5247DD1Q42094944-7A537E95-489F-4F6D-84E9-01973C83ED19Q42142499-777D3042-CEAB-4CC3-B784-73019F1DAAF0Q42412042-F9470F5B-AE92-4334-ABD8-0EB26FB9EB97
P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Xiaolan Zhao
@ast
Xiaolan Zhao
@en
Xiaolan Zhao
@es
Xiaolan Zhao
@nl
Xiaolan Zhao
@sl
type
label
Xiaolan Zhao
@ast
Xiaolan Zhao
@en
Xiaolan Zhao
@es
Xiaolan Zhao
@nl
Xiaolan Zhao
@sl
prefLabel
Xiaolan Zhao
@ast
Xiaolan Zhao
@en
Xiaolan Zhao
@es
Xiaolan Zhao
@nl
Xiaolan Zhao
@sl
P106
P21
P31
P496
0000-0002-8302-6905