Dimerization of MLH1 and PMS2 limits nuclear localization of MutLalpha.
about
ATM-mediated stabilization of hMutL DNA mismatch repair proteins augments p53 activation during DNA damageDNA mismatch repair: molecular mechanism, cancer, and ageingCharacterization of the interactome of the human MutL homologues MLH1, PMS1, and PMS2Structural, molecular and cellular functions of MSH2 and MSH6 during DNA mismatch repair, damage signaling and other noncanonical activitiesChallenges and pitfalls in HNPCC screening by microsatellite analysis and immunohistochemistry.Selective induction of DNA repair pathways in human B cells activated by CD4+ T cellsC-terminal fluorescent labeling impairs functionality of DNA mismatch repair proteins.Selenium compounds activate ATM-dependent DNA damage response via the mismatch repair protein hMLH1 in colorectal cancer cells.Apoptotic function of human PMS2 compromised by the nonsynonymous single-nucleotide polymorphic variant R20QComplex relationship between mismatch repair proteins and MBD4 during immunoglobulin class switch recombinationNuclear localization of human DNA mismatch repair protein exonuclease 1 (hEXO1)Modulation of microRNA processing by mismatch repair protein MutLα.Structure and function of the components of the human DNA mismatch repair system.An intact Pms2 ATPase domain is not essential for male fertilityHuman PMS2 deficiency is associated with impaired immunoglobulin class switch recombinationAlternative splicing regulates activation-induced cytidine deaminase (AID): implications for suppression of AID mutagenic activity in normal and malignant B cells.Reciprocal regulation of nuclear import of the yeast MutSalpha DNA mismatch repair proteins Msh2 and Msh6.Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repairTwo co-existing germline mutations P53 V157D and PMS2 R20Q promote tumorigenesis in a familial cancer syndrome.Pathological assessment of mismatch repair gene variants in Lynch syndrome: past, present, and future.Identification of Lynch syndrome mutations in the MLH1-PMS2 interface that disturb dimerization and mismatch repair.MLH1- and ATM-dependent MAPK signaling is activated through c-Abl in response to the alkylator N-methyl-N'-nitro-N'-nitrosoguanidine.The E705K mutation in hPMS2 exerts recessive, not dominant, effects on mismatch repair.Sub-cellular localization analysis of MSH6 missense mutations does not reveal an overt MSH6 nuclear transport impairment.Analysis of clinically relevant somatic mutations in high-risk head and neck cutaneous squamous cell carcinoma.The Changing Landscape of Lynch Syndrome due to PMS2 Mutations.Cancer risk assessment using genetic panel testing: considerations for clinical application.CRABS CLAW Acts as a Bifunctional Transcription Factor in Flower Development.
P2860
Q24564010-4EED17C4-5FFF-4C92-9DCF-2009FC04AE8FQ24647002-EBCC1874-2EDB-46BD-9E9E-B9D67E2B2B05Q28277364-37EDDB5E-2A68-4BD8-B82B-07C39136A0CCQ28285134-084DEB94-0CAE-4A52-A50E-F9B0586ACDC9Q33208352-A2F7D73B-2BB9-45EF-88FB-9838F684F4CDQ33778759-C20DF732-4B38-4A21-8884-0271C5EC2969Q34163755-0ED50C78-1C5C-4841-967F-D5863F0E8FACQ34236531-0C77A712-8AEA-43A5-B675-92844F952B4BQ34820495-FE5E1E1B-2C3E-445E-9C2B-0F96494B9272Q35036377-03111F56-9608-40DD-BCD9-EA4ABD5CDBE0Q35829272-9AD08ADF-42FC-40FB-89CD-99E9A3E52B39Q36009224-3B4A969B-7F17-470C-AF6F-3C026BE4A24DQ36521428-72E508B7-6AE6-444E-B358-B5C5BF34E7F4Q36614680-65FCD12A-B579-4711-9C18-A66DA1026680Q36946520-B6378C3A-468A-4CE6-8948-FDA842D4AF74Q37001985-B544F39F-C848-4F3D-8F51-885D545D5C8CQ37308166-6D3916D8-B64E-4B1E-97B7-9B195DC0530CQ37592729-46282CEF-090C-4471-BE17-A2BCD592D7B4Q37694831-AEF04068-FB08-44D8-9934-9F0DB3656F2CQ38029584-FF4024F0-A9A7-46F1-8A88-13596A889305Q39695410-312D8B0D-5464-453A-B017-E808F20C3521Q40084513-DD1CD093-D9FD-4BC7-8EE2-B986516691EDQ40222264-360AF4DB-82C8-4B1B-8E6A-4987626AA4B1Q47317424-C6FCA52C-C63C-48D7-9D46-67C56995117CQ48233207-69780BF8-C56C-47DB-ABB1-BE4AD7142208Q48332104-A70C9770-5A78-4AEB-9E66-D37EAE4DF872Q53292592-47135B3C-83A5-471E-B8CD-BA01E5F77529Q55423138-8CF974E8-49F8-4DAA-A8E1-B78B9F8618F2
P2860
Dimerization of MLH1 and PMS2 limits nuclear localization of MutLalpha.
description
2003 nî lūn-bûn
@nan
2003 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Dimerization of MLH1 and PMS2 limits nuclear localization of MutLalpha.
@ast
Dimerization of MLH1 and PMS2 limits nuclear localization of MutLalpha.
@en
Dimerization of MLH1 and PMS2 limits nuclear localization of MutLalpha.
@nl
type
label
Dimerization of MLH1 and PMS2 limits nuclear localization of MutLalpha.
@ast
Dimerization of MLH1 and PMS2 limits nuclear localization of MutLalpha.
@en
Dimerization of MLH1 and PMS2 limits nuclear localization of MutLalpha.
@nl
prefLabel
Dimerization of MLH1 and PMS2 limits nuclear localization of MutLalpha.
@ast
Dimerization of MLH1 and PMS2 limits nuclear localization of MutLalpha.
@en
Dimerization of MLH1 and PMS2 limits nuclear localization of MutLalpha.
@nl
P2093
P2860
P1476
Dimerization of MLH1 and PMS2 limits nuclear localization of MutLalpha.
@en
P2093
Jeffrey L Platt
Marilia Cascalho
Xiaosheng Wu
P2860
P304
P356
10.1128/MCB.23.9.3320-3328.2003
P407
P577
2003-05-01T00:00:00Z