Structure-based Design of High Affinity Peptides Inhibiting the Interaction of p53 with MDM2 and MDMX - Wikidata - awgldk - TriplyDB

Structure-based Design of High Affinity Peptides Inhibiting the Interaction of p53 with MDM2 and MDMX

Structure-based Design of High Affinity Peptides Inhibiting the Interaction of p53 with MDM2 and MDMX

http://www.wikidata.org/entity/Q27658148

about

MDM4 binds ligands via a mechanism in which disordered regions become structured Systematic Mutational Analysis of Peptide Inhibition of the p53–MDM2/MDMX Interactions Limitations of Peptide Retro-inverso Isomerization in Molecular Mimicry Stapled α−helical peptide drug development: A potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy Double Strain-Promoted Macrocyclization for the Rapid Selection of Cell-Active Stapled Peptides mRNA Display Selection of an Optimized MDM2-Binding Peptide That Potently Inhibits MDM2-p53 Interaction Simulating molecular mechanisms of the MDM2-mediated regulatory interactions: a conformational selection model of the MDM2 lid dynamics Probing Difference in Binding Modes of Inhibitors to MDMX by Molecular Dynamics Simulations and Different Free Energy Methods An observational study on the expression levels of MDM2 and MDMX proteins, and associated effects on P53 in a series of human liposarcomas Achieving cell penetration with distance-matching cysteine cross-linkers: a facile route to cell-permeable peptide dual inhibitors of Mdm2/Mdmx.The cis conformation of proline leads to weaker binding of a p53 peptide to MDM2 compared to trans.Novel pyrrolopyrimidine-based α-helix mimetics: cell-permeable inhibitors of protein−protein interactions Molecular basis of Bcl-X(L)-p53 interaction: insights from molecular dynamics simulations.Break CDK2/Cyclin E1 interface allosterically with small peptides.A natural small molecule harmine inhibits angiogenesis and suppresses tumour growth through activation of p53 in endothelial cells.Synthesis of cell-permeable stapled peptide dual inhibitors of the p53-Mdm2/Mdmx interactions via photoinduced cycloaddition Structural basis for inhibition of the MDM2:p53 interaction by an optimized MDM2-binding peptide selected with mRNA display.Autoinhibition of MDMX by intramolecular p53 mimicry Tethered ribozyme ligation enables detection of molecular proximity in homogeneous solutions.Regulation of MDM2 E3 ligase activity by phosphorylation after DNA damage.Targeting the p53 signaling pathway in cancer therapy - the promises, challenges and perils.Computational studies of difference in binding modes of peptide and non-peptide inhibitors to MDM2/MDMX based on molecular dynamics simulations.How To Design a Successful p53-MDM2/X Interaction Inhibitor: A Thorough Overview Based on Crystal Structures.Molecular dynamic simulation insights into the normal state and restoration of p53 function.Probing Origin of Binding Difference of inhibitors to MDM2 and MDMX by Polarizable Molecular Dynamics Simulation and QM/MM-GBSA Calculation Casein kinase 1α regulates an MDMX intramolecular interaction to stimulate p53 binding.Ligand binding mode prediction by docking: mdm2/mdmx inhibitors as a case study Monitoring Ligand-Induced Protein Ordering in Drug Discovery.The relationship between MDM2 expression and tumor thickness and invasion in primary cutaneous malignant melanoma.The structure-based design of Mdm2/Mdmx-p53 inhibitors gets serious Using peptides to study protein-protein interactions.New modalities in conformationally constrained peptides for potency, selectivity and cell permeation.Interactions of HIV-1 proteins as targets for developing anti-HIV-1 peptides.Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes.Rational, computer-enabled peptide drug design: principles, methods, applications and future directions.Peptides and peptidomimetics in the p53/MDM2/MDM4 circuitry - a patent review.MdmX is required for p53 interaction with and full induction of the Mdm2 promoter after cellular stress.PinaColada: peptide-inhibitor ant colony ad-hoc design algorithm.An α-Helix-Mimicking 12,13-Helix: Designed α/β/γ-Foldamers as Selective Inhibitors of Protein-Protein Interactions.Identification of small molecules affecting p53-MDM2/MDMX interaction by fluorescence polarization.

P2860

Q24316349-AC7878E2-7D17-455E-92F9-B6715E94349B Q27660219-65FC1167-AA81-4B41-9888-20C3ABC7F780 Q27660480-68EEDE5D-0E7B-4BA7-8C09-931E33B40031 Q27679680-F8B25836-2409-4C45-ADD5-E43327BFEA01 Q27703615-DD6D4937-5C68-4666-8BE0-DDF9FE36E1B6 Q28386936-208E00C4-3A4F-4F6D-A795-64402ED4CEF1 Q28481334-F06F69B7-8C40-4522-92B7-27FC0EB1C101 Q28550543-D726B9B2-4CD7-46EF-A907-6F170CC52DDE Q33640890-1C650E89-DEB5-4573-B326-BDBD332BDEBC Q33674529-E658FDD8-AEBB-4E02-BA0C-1E4737913B7F Q33727589-315B96B0-44DD-43BE-AFAF-3CF96BD9BD1E Q33775959-37AFA810-4135-4FD2-A1DF-CE46422C8744 Q34062295-8A46093E-45B2-4F07-933A-BB1CED2621E3 Q34301581-698DADCF-0E4F-4762-A58E-62E278B13B48 Q34540424-410124EA-7857-401F-9D8D-E3C2ED66E978 Q34670518-CC7908E3-7CF4-4980-9B67-DE3BFF1805B7 Q35295410-FC5E396E-46BF-46F7-885A-E007096664AC Q35485193-96B35092-1D02-4506-B1EC-509B6DF1C95A Q35523502-31238492-B684-4C29-96DE-1BABF0020D2A Q35599086-17AA6478-8AB5-46BB-8F57-4909EE7A4F5C Q35795073-DA9CC281-D25C-470E-BB2A-9445E752C603 Q35795880-89A5ECEE-084B-4F5D-A9BC-0FA0331EF02D Q35871210-9FD35A6F-466D-4F80-A5BB-831683D3DE0D Q36202281-0A0083B1-BD1A-49D0-A664-CAB5E6927289 Q36329555-DCA4A116-82FF-41A7-A406-8B9EDD5C820A Q36397318-27617FF8-795E-4790-8477-29091EA51CF2 Q36579823-54D9BD8E-7ED2-419D-8CE9-9250494F3489 Q36782842-24D4C72F-C3F8-4771-BBC5-48D693C46810 Q36789792-53CE4528-6A5C-4693-8B63-299B73A56B43 Q37845797-2A9498D5-B414-4BAA-9B4A-9D5D26FF5371 Q37855887-C01BBA78-5797-4E19-AD56-D20A3E35839C Q38104757-A88543D8-BEB7-46BE-8733-92DEE8EF1279 Q38524164-002EB982-B139-4FA9-A118-8F13990AA805 Q38539666-409FDF7D-842E-402F-9081-5846C6E5ABB3 Q38618616-74BC87D7-5235-485B-8CDB-EAA3ED185EC0 Q38948352-C9AE0E85-1F5E-4256-BF97-EF7B46BA1F08 Q39404029-248AC89C-2640-46B5-BAC9-58B144435096 Q39788518-259AE3D2-7BA3-4978-B3AE-98155F2883EE Q41034048-1552E1AA-FD74-48DD-9BD8-4A1E7F58996A Q42581692-55B12DEF-DA97-4C70-B2EA-273DDBDB4D9F

P2860

Structure-based Design of High Affinity Peptides Inhibiting the Interaction of p53 with MDM2 and MDMX

http://www.wikidata.org/entity/Q27658148

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Structure-based Design of High ...... tion of p53 with MDM2 and MDMX

@ast

Structure-based Design of High ...... tion of p53 with MDM2 and MDMX

@en

Structure-based Design of High ...... tion of p53 with MDM2 and MDMX

@nl

type

label

Structure-based Design of High ...... tion of p53 with MDM2 and MDMX

@ast

Structure-based Design of High ...... tion of p53 with MDM2 and MDMX

@en

Structure-based Design of High ...... tion of p53 with MDM2 and MDMX

@nl

prefLabel

Structure-based Design of High ...... tion of p53 with MDM2 and MDMX

@ast

Structure-based Design of High ...... tion of p53 with MDM2 and MDMX

@en

Structure-based Design of High ...... tion of p53 with MDM2 and MDMX

@nl

P1433

Q27658148-17513C85-BA17-4F90-8A86-9F2439D80674

P1476

Q27658148-D67349AF-D6EF-4BC4-8A27-0177E587327A

P2093

Q27658148-6B34EC2B-8E96-4443-B60F-EBE0E1E78FD5

Q27658148-81FABDD3-392C-42E2-B5C9-9A43DA2BD9B5

Q27658148-90AEAD76-842C-4C23-8143-D8005757BD7D

Q27658148-96A20A56-58FE-4D8A-A925-EC9249BA033F

Q27658148-DBD93E99-CC91-43A9-96D0-2C6D1423CF87

Q27658148-F11197AD-709B-4DF3-A42D-8785C46A841A

Q27658148-F24F9A07-088A-4737-8A68-C9FC1C08931A

Q27658148-FF26ACDD-76E6-41D6-8157-C7ADC36F4860

P2860

Q27658148-02DE0C7D-A613-4E67-9569-74FC48BA9105

Q27658148-0AFEF43E-FDD5-4949-9DE2-5670167A0A46

Q27658148-1CAB506C-DB69-4C32-B459-F059F35F2297

Q27658148-20EB45C0-7B82-4C5B-B8F7-BDF7AFBB7D78

Q27658148-2852FB16-6DE2-46AD-BE86-9A251A1E5B78

Q27658148-2D6237AB-AEF9-4E2F-8EDE-BF52D4ABD745

Q27658148-34D8B30D-8055-4B46-8E10-0FEBD78B4A8D

Q27658148-388DF8C5-851F-4E2D-9C83-E10873581AD0

Q27658148-38EAD53F-4615-484E-9FFF-F811249BDB40

Q27658148-3F225939-6A84-4A54-BC22-0770898622F7

P304

Q27658148-0FA0F5D2-C1A5-411B-894F-BA3F9758D967

P31

Q27658148-0B89DE5C-B50E-4BF1-B7E5-D0EB2077AF82

P3181

Q27658148-5CDB3E00-50F4-4DC5-9140-89B164E5F78B

P356

Q27658148-A33D0A17-A5CF-41AE-BE5C-897D7DD8B04E

P407

Q27658148-69FF606F-7D80-46D8-B118-797548694E77

P433

Q27658148-56F28BFF-CBFD-42C4-8981-8A72C7F7250F

P478

Q27658148-A5BEA5BF-58C8-4988-9008-F33B98A88C97

P577

Q27658148-409ACF76-47A9-42AA-99D1-BF189A319FE7

P698

Q27658148-93780288-B67B-4A1B-8309-E84608C0955E

P921

Q27658148-D02B0028-7B08-45B5-8CD3-1774501D90BE

P932

Q27658148-CD3A292E-C1A4-4DB7-BAF0-AAD4C69F04AF

P3181

P356

JBC.M109.073056

P1433

Journal of Biological Chemistry

P1476

Structure-based Design of High ...... tion of p53 with MDM2 and MDMX

@en

P2093

Agnieszka Kasprzak

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

Baozong Li

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

Ernst Schönbrunn

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

Jason Phan

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

Jiandong Chen

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

Said Sebti

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

Wayne Guida

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

Zhenyu Li

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

P2860

Efficient p53 activation and apoptosis by simultaneous disruption of binding to MDM2 and MDMX

Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain

MDMX regulation of p53 response to ribosomal stress

MDMX: a novel p53-binding protein with some functional properties of MDM2

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

In vivo activation of the p53 pathway by small-molecule antagonists of MDM2

Molecular basis for the inhibition of p53 by Mdmx

Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain

Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX

P304

2174-83

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

P31

scholarly article

P3181

4259209

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

P356

10.1074/JBC.M109.073056

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

P407

P433

3

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

P478

285

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

P577

2010-01-15T00:00:00Z

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

P698

19910468

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

P921

P932

2804373

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