Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain - Test2 - elhamkhani - TriplyDB

Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain

Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain

http://www.wikidata.org/entity/Q27660302

about

Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1 PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53 An unexpected journey: lysine methylation across the proteome Solution Structure and Molecular Interactions of Lamin B Receptor Tudor Domain Lysine methylation-dependent binding of 53BP1 to the pRb tumor suppressor Translational roles of elongation factor 2 protein lysine methylation A new type of protein lysine methyltransferase trimethylates Lys-79 of elongation factor 1A p53 transactivation and the impact of mutations, cofactors and small molecules using a simplified yeast-based screening system Cation-π interactions of methylated ammonium ions: a quantum mechanical study.Mutant TP53 posttranslational modifications: challenges and opportunities.Protein binding specificity versus promiscuity.Keeping it in the family: diverse histone recognition by conserved structural folds Small-molecule ligands of methyl-lysine binding proteins: optimization of selectivity for L3MBTL3.An acetyl-methyl switch drives a conformational change in p53.Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1 A role for the p53 tumour suppressor in regulating the balance between homologous recombination and non-homologous end joining.Drug discovery toward antagonists of methyl-lysine binding proteins Lysine methylation: beyond histones.Tudor: a versatile family of histone methylation 'readers'.Mind the methyl: methyllysine binding proteins in epigenetic regulation.A Structural Perspective on Readout of Epigenetic Histone and DNA Methylation Marks.c-Fos-dependent miR-22 targets MDC1 and regulates DNA repair in terminally differentiated cells.Optimization of a synthetic receptor for dimethyllysine using a biphenyl-2,6-dicarboxylic acid scaffold: insights into selective recognition of hydrophilic guests in water.

P2860

Q24303435-E59EC45A-BF42-438A-B4C3-120DEF9B9369 Q24594648-23AD6F44-DC2D-4458-A34E-35F8C47BDA84 Q26864659-F601B4DA-4968-480F-BA6B-D8E34F7B5351 Q27675370-2DFCF89E-FAC0-408B-ACC5-BB767F7EAEE7 Q27684769-51B5E74A-AE9E-48ED-B342-DECD75A32F6C Q27933550-B344BB2D-3A21-4BC8-87F0-1DF853D4D980 Q27939199-6FF30F78-2244-42A4-8EC8-A00DB5FA6E83 Q28478414-64DC58EB-EFB1-40FA-A6B1-779094BAF4E6 Q33754213-BE294A3E-3A2E-4825-87D5-2B099320C4A4 Q33818479-6FB9BF39-69C8-4E3B-9D4D-FC992389AF34 Q34149308-F9C4BEA7-2FDF-496E-B19D-86FA1DC63443 Q34336457-647C3C14-744D-4AA4-9D82-D28FCBD66133 Q34990803-A03111B7-E8A6-46C4-9DE7-28FAA1E8E142 Q35050674-3F995CE0-EAA6-4C05-A155-21B120E2CD0A Q35063951-2EF696D0-A8E1-44F5-B027-2E54742BAC2E Q37299259-6F3A278C-E6A6-49B8-80EA-7550E0559A9C Q37965165-E024A616-EA41-45E4-8A00-D6F3DFE6A342 Q37970950-64CDB86A-FB16-45C3-A967-2C833A92212E Q38137526-634A5D36-239D-4F21-805A-7B51D432FC83 Q38180674-7EBD41CA-8CC6-4CB7-BA6A-DCEDD9DFDED6 Q38756663-51F42CCC-52BF-4CD0-99FD-F0A562C566D5 Q41471528-DF6383D0-1DF5-4768-A949-D2DDDAB3B4C0 Q47849445-B4E5D2CF-5055-4A1D-B2D1-81469305BFD9

P2860

Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain

http://www.wikidata.org/entity/Q27660302

description

2010 nî lūn-bûn

@nan

2010 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年学术文章

@wuu

2010年学术文章

@zh-cn

2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

@zh-sg

2010年學術文章

@yue

name

Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain

@ast

Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain

@en

Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain

@nl

type

label

Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain

@ast

Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain

@en

Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain

@nl

prefLabel

Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain

@ast

Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain

@en

Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain

@nl

P1433

Q27660302-40FD7AA6-D4D6-4B1F-8738-5000FB5CA5B8

P1476

Q27660302-4B0B4E93-6E00-4DBC-B0F7-910EAAB28C22

P2093

Q27660302-26A1F788-3F90-4B60-A9FF-836DD8E80C29

Q27660302-43B87BD2-7492-432C-9A53-76F24D3C4E68

Q27660302-44F49EDA-3C09-454A-8B75-55BBE55BA59E

Q27660302-7CB04C0F-A4CC-4897-AECA-EAF44016EF69

Q27660302-ACA89E30-833E-431F-8CD1-798C750D5DC4

P2860

Q27660302-06D5C3DE-CF73-488C-90E5-F0B6BF15D0C2

Q27660302-149DDE27-0B91-4078-85CD-478DC788DCAE

Q27660302-1982BAC5-150C-46E7-B31F-0E88755447F6

Q27660302-1AEA8D95-95DF-4973-99CA-2A7A99E7E2A3

Q27660302-21B04FE0-07B3-4774-A9E0-92D3C4A354F2

Q27660302-25300770-98B6-49FC-B99E-9877CCE843FF

Q27660302-30396E27-0896-463A-9945-CEA05A9DB8FB

Q27660302-3AD70D97-54CC-443D-AFC4-CA2FFD39A450

Q27660302-4721B962-6029-4978-AC4E-77DAAC9ECB55

Q27660302-488A66B5-ADA7-475E-8933-AB22E33396F0

P304

Q27660302-ADACCFD9-4729-459C-9366-CD97F1638202

P31

Q27660302-9C02DE3C-8DB5-4E7A-B8E8-F883C5A2F057

P3181

Q27660302-F777773C-F0AB-48FC-9EEA-7A3C7BCACFC1

P356

Q27660302-43895B25-E8DA-4350-B940-E46F55314C13

P407

Q27660302-007487CA-3867-4641-AAAA-B6FD6D5DC62F

P433

Q27660302-DA6BB2CD-F8CA-4439-B332-6ED0246587B4

P478

Q27660302-1050324D-CD7D-4AF3-9A25-F67D2A67B5F8

P50

Q27660302-007D0BB3-3734-4791-983B-6FC136DA545B

Q27660302-AB678E1D-8F6A-410A-B1D7-29521A983D6D

Q27660302-DF31BEAF-84C3-4246-B60C-6F159E47B9BE

Q27660302-FA48E54C-AAEF-469B-885A-BBB8E263D5E1

P577

Q27660302-4CF2872E-FA0D-4BF4-83FF-1E5BC6C81376

P5875

Q27660302-4D144FC0-7F17-4D03-8DA5-0BBC7D502319

P698

Q27660302-44A23224-F49F-429C-B064-87CD793AD723

P932

Q27660302-12765C98-88F1-4A6A-9081-69DD8A5E86CD

P3181

P356

J.JMB.2010.03.024

P1433

Journal of Molecular Biology

P1476

Structural insight into p53 recognition by the 53BP1 tandem Tudor domain

@en

P2093

Ettore Appella

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

Ioulia Kachirskaia

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

Jay C Nix

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

Ryo Hayashi

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

Siddhartha Roy

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

P2860

p53 is regulated by the lysine demethylase LSD1

Regulation of p53 activity through lysine methylation

Repression of p53 activity by Smyd2-mediated methylation

Modulation of p53 function by SET8-mediated methylation at lysine 382

ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression

Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair

Structural Basis for Lower Lysine Methylation State-Specific Readout by MBT Repeats of L3MBTL1 and an Engineered PHD Finger

Coot: model-building tools for molecular graphics

The finer things in X-ray diffraction data collection

Likelihood-enhanced fast rotation functions

P304

489-496

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

P31

scholarly article

P3181

3739295

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

P356

10.1016/J.JMB.2010.03.024

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

P407

P433

4

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

P478

398

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

P50

Catherine Musselman

Tatiana G Kutateladze

P577

2010-03-20T00:00:00Z

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

P5875

42388575

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

P698

20307547

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

P932

2865857

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