Determination of protein-DNA binding constants and specificities from statistical analyses of single molecules: MutS-DNA interactions - Wikidata - awgldk - TriplyDB

Determination of protein-DNA binding constants and specificities from statistical analyses of single molecules: MutS-DNA interactions

Determination of protein-DNA binding constants and specificities from statistical analyses of single molecules: MutS-DNA interactions

http://www.wikidata.org/entity/Q24815928

about

Single-molecule views of MutS on mismatched DNA.ComEA is essential for the transfer of external DNA into the periplasm in naturally transformable Vibrio cholerae cells Modulation of the DNA-binding activity of Saccharomyces cerevisiae MSH2-MSH6 complex by the high-mobility group protein NHP6A, in vitro Mechanism of MutS searching for DNA mismatches and signaling repair Dynamic basis for one-dimensional DNA scanning by the mismatch repair complex Msh2-Msh6.Label-free, atomic force microscopy-based mapping of DNA intrinsic curvature for the nanoscale comparative analysis of bent duplexes.Activation-induced deaminase, AID, is catalytically active as a monomer on single-stranded DNA.Substrate binding pocket residues of human alkyladenine-DNA glycosylase critical for methylating agent survival Saccharomyces cerevisiae Msh2-Msh6 DNA binding kinetics reveal a mechanism of targeting sites for DNA mismatch repair.Direct visualization of asymmetric adenine-nucleotide-induced conformational changes in MutL alpha.The UvrD303 hyper-helicase exhibits increased processivity.The effect of increasing numbers of repeats on TAL effector DNA binding specificity MutS switches between two fundamentally distinct clamps during mismatch repair.Single molecule studies of DNA mismatch repair.Lesion search and recognition by thymine DNA glycosylase revealed by single molecule imaging.New insights into the regulatory mechanisms of ppGpp and DksA on Escherichia coli RNA polymerase-promoter complex.Biochemical analysis of the human mismatch repair proteins hMutSα MSH2(G674A)-MSH6 and MSH2-MSH6(T1219D)Structure and specificity of the RNA-guided endonuclease Cas9 during DNA interrogation, target binding and cleavage Cooperative cluster formation, DNA bending and base-flipping by O6-alkylguanine-DNA alkyltransferase.Atomic force microscopy captures the initiation of methyl-directed DNA mismatch repair.The PIN domain of EXO1 recognizes poly(ADP-ribose) in DNA damage response.Poly(ADP-Ribose) Mediates the BRCA2-Dependent Early DNA Damage Response.Single molecule detection of PARP1 and PARP2 interaction with DNA strand breaks and their poly(ADP-ribosyl)ation using high-resolution AFM imaging.AFM studies of lambda repressor oligomers securing DNA loops Imaging of DNA and Protein-DNA Complexes with Atomic Force Microscopy.Single-molecule analysis reveals two separate DNA-binding domains in the Escherichia coli UvrA dimer.Strand-specific recognition of DNA damages by XPD provides insights into nucleotide excision repair substrate versatility.Functional characterization and atomic force microscopy of a DNA repair protein conjugated to a quantum dot.Symmetric curvature descriptors for label-free analysis of DNA.DNA substrate preparation for atomic force microscopy studies of protein-DNA interactions.Mismatch binding, ADP-ATP exchange and intramolecular signaling during mismatch repair.Atomic force microscopy captures MutS tetramers initiating DNA mismatch repair.Dual role of MutS glutamate 38 in DNA mismatch discrimination and in the authorization of repair.Mechanically Induced Trapping of Molecular Interactions and Its Applications.Extracting physical chemistry from mechanics: a new approach to investigate DNA interactions with drugs and proteins in single molecule experiments.Studying protein-DNA interactions using atomic force microscopy.Dynamics of MutS-mismatched DNA complexes are predictive of their repair phenotypes Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair.Single-molecule FRET TACKLE reveals highly dynamic mismatched DNA-MutS complexes.Conservation and Divergence in Nucleotide Excision Repair Lesion Recognition.

P2860

Q26999680-60BC185C-4CDF-4A9E-A2F2-5C8CABAF2D3F Q27317580-5E354BC9-DE98-415A-914B-7173BC6D4D12 Q27931842-D416228C-4C42-435E-B4EA-B00755A42408 Q28756121-C2826D6E-EEC2-4C65-84EE-2190AD105F1E Q30496957-B2D3F6D6-DE89-4FC5-9167-0DFB764D650C Q30514563-70101B9E-F01C-4138-BCA5-04087CE83BC4 Q33299999-ACEA9360-FD3D-40C3-AF5A-148D0E33B3E3 Q33360502-B2BDBA71-2440-42A3-BA29-973D2A9266A1 Q33640393-391C1815-7B68-4404-9547-03A80C2C3574 Q33645614-7CFA6352-A447-4C30-ADBE-DC91F0E6C725 Q33761309-9EAAE3FF-DB62-404C-9E89-1971D6888E10 Q33879046-97C7ACE9-3FEB-49FF-B361-FD6B1232E99E Q34698570-0CF35275-9C69-42E6-B8AB-C369C0289BD9 Q35027619-389B5B46-663B-4029-8C6E-294902E4C80B Q35171647-9F5C6EC6-870C-4213-9D6E-0BCD42921F94 Q35656820-A808460B-F078-4283-8839-8FDCD66319F7 Q35880032-10AC28C1-0BFE-4868-B4AA-75B848A69B41 Q36160691-29D2ED3C-8810-4D27-BACD-61E38A36C861 Q36280616-596A7F9B-2F3A-4144-BD99-9997B75039F6 Q36296925-CF9352E4-3201-4365-BA88-DBB3B319051B Q36370917-E178FAC3-8AFE-4169-B644-86B4F34A6124 Q36694981-070813A7-CA1D-4558-AEE3-37DBE7E5BE78 Q36775498-7EB17BFF-14AD-4DE8-9536-BE185263A208 Q36809173-1787C1B9-D7F0-4EB6-AB7C-604FC7FB65D6 Q36991424-015F5191-C663-4654-8450-8969DE53AB45 Q37149796-23FAFD33-9DFB-4FEC-A159-294484FA6CC5 Q37563531-187FB6A1-21B7-42E5-94CB-76045FDB765D Q37614786-FDD41977-8053-490D-A961-BFD1738E5AFD Q37734631-BAB16CE4-C6FD-4B06-ABF2-B545BA1A9B3A Q38166320-9A625C32-409E-4407-A469-67F546607C17 Q38254881-EE80CCC8-5957-473D-B797-78C428C87A8C Q38254948-A7300728-C54D-4B5A-AE48-D6565859D0AF Q38316881-AAC82E4E-A944-4F9E-AA72-35A1A8BB9621 Q38389868-48501D61-A0FF-49D3-9F21-244D3C493363 Q38569444-F51AF8F7-0B5C-4D9F-B1BB-E36DDAFE88B7 Q38663291-B8A11E9C-ACC4-4D09-9B05-8658BB6DDE0C Q38739461-213B0CD3-715F-4836-853C-9877738BEC86 Q38750909-F62B2AAD-F1FC-4EDE-88E0-534A0835B6B2 Q40124687-875BF530-873C-487C-9B76-F59DF68B178F Q41002702-9632D154-17B6-4165-9A4D-EF478B24FA78

P2860

Determination of protein-DNA binding constants and specificities from statistical analyses of single molecules: MutS-DNA interactions

http://www.wikidata.org/entity/Q24815928

description

2005 nî lūn-bûn

@nan

2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Determination of protein-DNA b ...... lecules: MutS-DNA interactions

@ast

Determination of protein-DNA b ...... lecules: MutS-DNA interactions

@en

Determination of protein-DNA b ...... lecules: MutS-DNA interactions

@nl

type

label

Determination of protein-DNA b ...... lecules: MutS-DNA interactions

@ast

Determination of protein-DNA b ...... lecules: MutS-DNA interactions

@en

Determination of protein-DNA b ...... lecules: MutS-DNA interactions

@nl

prefLabel

Determination of protein-DNA b ...... lecules: MutS-DNA interactions

@ast

Determination of protein-DNA b ...... lecules: MutS-DNA interactions

@en

Determination of protein-DNA b ...... lecules: MutS-DNA interactions

@nl

P1433

Q24815928-A4259342-80B1-454D-998A-053170B00E2E

P1476

Q24815928-AE9CB027-B09B-4A85-8FD4-F85B6841AF68

P2093

Q24815928-3B0EFC36-068F-4673-BEAE-B0C09FB71E1A

Q24815928-51521B39-7B05-41EA-A459-BAE8B14AEE5A

Q24815928-6BF8866A-1A15-47DF-8762-CBDFE8C9508D

Q24815928-77BD65B9-AAC6-4406-AF0B-9B109923AAC8

Q24815928-AACA695D-617A-427A-A7A8-AF57B64B3910

P2860

Q24815928-1B6A47AB-58E0-41B8-98A7-585C6D11BD94

Q24815928-21ACFC0D-6C43-427B-80F7-2C291113E2AD

Q24815928-237C6DD7-09AF-420E-9ACE-9A8504CAB7DB

Q24815928-259F8B71-11C8-4823-B31E-FE0CBAA92B13

Q24815928-29755E44-52A0-4625-9BCD-A69472CF35B3

Q24815928-321F13A9-FC72-4FAD-ABD1-A49F3D73A52B

Q24815928-36E3CE48-1D70-47F4-9193-C31A19068C28

Q24815928-525EFEA4-47A8-4A1B-A947-AAF5629A84C6

Q24815928-5318B0C2-FA25-449F-85A6-BB94EDB85F23

Q24815928-5754CC11-3E8B-4C26-B9DE-F7E319B01A66

P304

Q24815928-1898EFA1-6A16-4116-ADBB-519DC3372534

P31

Q24815928-21BBAB6A-8469-40F9-8D3C-D743A2F71052

P3181

Q24815928-6814AD9B-05A2-4AD2-88A6-A09394DD6701

P356

Q24815928-5535496C-CB5E-4460-B9F0-4177DBCE68EE

P407

Q24815928-0AD97F7C-A5CB-448D-8D40-EC8A2F15B8F8

P433

Q24815928-9A60A66F-5697-4A23-8CDA-F9898359897E

P478

Q24815928-6C7DB7BC-4DE9-4CE0-A6B8-25168F559BC4

P577

Q24815928-79C2D81D-007B-4F2D-A0C4-6BFFB9299CC7

P5875

Q24815928-69EDF0F6-B9DA-45F8-9235-A13F87474C0B

P698

Q24815928-89F0629A-0296-4179-8D55-B68CFCD90820

P921

Q24815928-3E9D9F27-4DE0-47A0-B41E-42A94D891B26

P932

Q24815928-951F72B4-242E-41B9-B5F5-895B8774361D

P3181

P356

P1433

Nucleic Acids Research

P1476

Determination of protein-DNA b ...... lecules: MutS-DNA interactions

@en

P2093

Chunwei Du

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

Dorothy A Erie

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

Lauryn E Sass

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

Peggy Hsieh

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

Yong Yang

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

P2860

Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA

The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch

Structures of Escherichia coli DNA mismatch repair enzyme MutS in complex with different mismatches: a common recognition mode for diverse substrates

The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch

Mismatch repair in replication fidelity, genetic recombination, and cancer biology

Oligomerization of a MutS mismatch repair protein from Thermus aquaticus.

A statistical thermodynamic model applied to experimental AFM population and location data is able to quantify DNA-histone binding strength and internucleosomal interaction differences between acetylated and unacetylated nucleosomal arrays

The XPC-HR23B complex displays high affinity and specificity for damaged DNA in a true-equilibrium fluorescence assay.

Probing protein-DNA interactions by unzipping a single DNA double helix.

Molecular mechanisms of DNA mismatch repair.

P304

4322-4334

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

P31

scholarly article

P3181

1526363

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

P356

10.1093/NAR/GKI708

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

P407

P433

13

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

P478

33

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

P577

2005-08-01T00:00:00Z

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

P5875

7685843

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

P698

16061937

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

P921

P932

1182163

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