Solution Structure of a Hydrocarbon Stapled Peptide Inhibitor in Complex with Monomeric C-terminal Domain of HIV-1 Capsid - Wikidata - wikimedia - TriplyDB

Solution Structure of a Hydrocarbon Stapled Peptide Inhibitor in Complex with Monomeric C-terminal Domain of HIV-1 Capsid

Solution Structure of a Hydrocarbon Stapled Peptide Inhibitor in Complex with Monomeric C-terminal Domain of HIV-1 Capsid

http://www.wikidata.org/entity/Q27650342

about

HIV type 1 Gag as a target for antiviral therapy Virus maturation as a new HIV-1 therapeutic target All-atom model for stabilization of alpha-helical structure in peptides by hydrocarbon staples.Stapled BH3 peptides against MCL-1: mechanism and design using atomistic simulations Residues in the HIV-1 capsid assembly inhibitor binding site are essential for maintaining the assembly-competent quaternary structure of the capsid protein X-ray structures of the hexameric building block of the HIV capsid.HIV Capsid is a Tractable Target for Small Molecule Therapeutic Intervention Inhibition of oncogenic Wnt signaling through direct targeting of -catenin Structure of a Monomeric Mutant of the HIV-1 Capsid Protein Rationally designed interfacial peptides are efficient in vitro inhibitors of HIV-1 capsid assembly with antiviral activity Hydrocarbon-stapled peptides: principles, practice, and progress The capsid protein of human immunodeficiency virus: designing inhibitors of capsid assembly.Novel approaches to inhibiting HIV-1 replication.Virtual screening based identification of novel small-molecule inhibitors targeted to the HIV-1 capsid.Bridged beta(3)-peptide inhibitors of p53-hDM2 complexation: correlation between affinity and cell permeability.Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera.Biophysical characterization of the feline immunodeficiency virus p24 capsid protein conformation and in vitro capsid assembly.Cullin3-BTB interface: a novel target for stapled peptides Helix stabilization of amphipathic peptides by hydrocarbon stapling increases cholesterol efflux by the ABCA1 transporter.Synthetic mimetics of protein secondary structure domains HIV-1 Gag as an Antiviral Target: Development of Assembly and Maturation Inhibitors.Novel structures of self-associating stapled peptides.Identification of a small molecule HIV-1 inhibitor that targets the capsid hexamer.Stapling mimics noncovalent interactions of γ-carboxyglutamates in conantokins, peptidic antagonists of N-methyl-D-aspartic acid receptors Bis-azobenzene crosslinkers for photocontrol of peptide structure.HIV-1 Capsid Inhibitors as Antiretroviral Agents Characterization of the in vitro HIV-1 capsid assembly pathway.Dual-acting stapled peptides target both HIV-1 entry and assembly New approaches for antiviral targeting of HIV assembly.Stabilized helical peptides: overview of the technologies and therapeutic promises.Stapled peptide inhibitors of RAB25 target context-specific phenotypes in cancer.IKKγ-Mimetic Peptides Block the Resistance to Apoptosis Associated with Kaposi's Sarcoma-Associated Herpesvirus Infection.Z-Selective olefin metathesis on peptides: investigation of side-chain influence, preorganization, and guidelines in substrate selection Antimicrobial activity and stability of stapled helices of polybia-MP1.Mono-substitution effects on antimicrobial activity of stapled heptapeptides.Inhibitors of the HIV-1 capsid, a target of opportunity.A new i, i + 3 peptide stapling system for α-helix stabilization.

P2860

Q24614498-A75EC103-84BF-464A-8DB0-537330C18CA3 Q24642446-885B7FF3-B4EF-4985-8C04-20742B35DAAA Q24645116-83DBCE8F-34FC-4DFB-9815-012385A5E00D Q27321588-5615DCCF-5351-4A73-AB2A-C7646F76BDFE Q27651983-B46B9FC1-7DB0-48E5-B99E-52869F266CBE Q27655910-9A4DBC19-BFBB-4E0A-8089-9D457C94A338 Q27666355-3A232E07-85F7-4BF0-9F5E-5E83DA6A190E Q27674587-9AE245C8-9900-45E3-8B16-D656F18BF518 Q27675009-F39F1E49-3C71-4645-B696-CE3566D393E3 Q28476840-20E8A461-ED7A-4987-B52C-8455DEA2A72F Q28542025-B596270A-9A23-4156-9A19-F1ECDA060F0A Q33510254-AE6A55D3-E90C-4A9B-8211-964297C27534 Q33624690-D70546B8-37E2-44CD-BB50-497C8AEB0AE3 Q33774977-F9511F78-6023-4AE3-B7BD-58B8671C56E6 Q33782756-BC721970-7179-405A-8A49-7BF5BFD5E88C Q34242529-81CA5985-3844-4AA6-9AB1-7EE89CAB9379 Q34606804-8A3138A4-FE65-4537-B357-45F83E379666 Q35596110-3DA7035E-43A8-4CCF-B2DD-F38281AF8EB9 Q35660283-FE58B1A7-0201-4DE0-B975-42E80BC0D7AA Q35688001-7C8FB40A-18D1-4431-A2B0-085BF9AD8260 Q35761626-003830E0-7AD9-4D1C-ACC6-3A8471A2DB9C Q35835917-FBF81B70-413D-45CB-81FC-9E8167C88247 Q35889216-68B2E731-0F84-4EC0-85FF-C56E3E964461 Q36017011-D9347E9C-F36D-41BF-A01E-BBF39CDE0BE3 Q36453001-D4A10B86-BC20-4E2C-B152-0058696E03BC Q36672006-E9B75746-240F-4448-BAD3-C445126433B6 Q37155570-5637B3F0-81A4-4C88-BE37-DF43EBB83490 Q37348096-EB1A12C5-7315-4EB3-A3B4-BC34C3EF8976 Q37901613-32638995-B40B-420C-BC7A-C6FA4AAE9E5D Q38014489-39B63307-EC35-4492-A250-88C5AB51FBA4 Q41689815-E77059C9-4691-4DA7-B12B-4068163FA395 Q41933434-13EAD729-DE98-4FD4-9892-E3EF1DEE402E Q42545827-4B333265-C574-453D-B228-E5A6357518ED Q47637115-3A5EEC21-98FA-415D-B3CF-47D4B0E081D1 Q48088935-4D7C80F5-2615-4021-9995-164C2DB37FF2 Q54204420-85499586-D0A9-4E87-A38B-1A55E6819542 Q54548513-31386040-5E4E-4ADC-8F56-AF6A9EE2D9EC

P2860

Solution Structure of a Hydrocarbon Stapled Peptide Inhibitor in Complex with Monomeric C-terminal Domain of HIV-1 Capsid

http://www.wikidata.org/entity/Q27650342

description

2008 nî lūn-bûn

@nan

2008 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Solution Structure of a Hydroc ...... erminal Domain of HIV-1 Capsid

@ast

Solution Structure of a Hydroc ...... erminal Domain of HIV-1 Capsid

@en

Solution Structure of a Hydroc ...... erminal Domain of HIV-1 Capsid

@nl

type

label

Solution Structure of a Hydroc ...... erminal Domain of HIV-1 Capsid

@ast

Solution Structure of a Hydroc ...... erminal Domain of HIV-1 Capsid

@en

Solution Structure of a Hydroc ...... erminal Domain of HIV-1 Capsid

@nl

prefLabel

Solution Structure of a Hydroc ...... erminal Domain of HIV-1 Capsid

@ast

Solution Structure of a Hydroc ...... erminal Domain of HIV-1 Capsid

@en

Solution Structure of a Hydroc ...... erminal Domain of HIV-1 Capsid

@nl

P1433

Q27650342-1DCF0948-E419-4529-AC1D-5A0B710D11D9

P1476

Q27650342-5B04799C-2849-4F59-967E-E06FE6600F94

P2093

Q27650342-4618E06C-5B1C-400E-8E8D-F8A20DC78DCC

Q27650342-5AC364B5-472C-4780-A3C7-CED2F4C61894

Q27650342-829A28F2-1C0B-4796-9941-C7F01CE7B290

P2860

Q27650342-0C6DFB26-0290-4C58-A4D7-6038BDB5BF6E

Q27650342-11F83E77-0FA3-4A8F-9F77-1B2172A6FFA7

Q27650342-320458A1-E4E0-419F-9CC1-D6DA12E17977

Q27650342-3B144673-539E-49B2-8D53-B79958FE167D

Q27650342-4D869EB3-2402-4F73-8A67-6B1074D83261

Q27650342-51B70E17-5EAB-43B2-82D0-872C47B22613

Q27650342-53157E54-EDDD-423E-8AEA-CDA8C6210B57

Q27650342-54AF9408-DD40-4547-808A-9068D7B8AE3E

Q27650342-583EDC46-3B8B-4B5A-BB03-8C134CFE7DF7

Q27650342-73E93E7F-7B90-4025-9A26-44D49F4DF8DD

P304

Q27650342-F8714B70-0BE4-437C-9FD2-FC96C207DFCB

P31

Q27650342-D9014F1D-2047-4BD5-85DC-233BB1A85891

P356

Q27650342-4B828419-7AE3-44DB-8E9D-F1CDF4B498B6

P407

Q27650342-313F66EC-005D-428A-B0FB-283B7F6A8178

P433

Q27650342-E67BE543-A2C6-418D-B174-22E71D51C9AF

P478

Q27650342-FDDB004D-0977-40BE-A316-D0E1F8BECC8D

P50

Q27650342-CEA769BA-FFAC-4638-B4DF-3A05568DFCE2

P577

Q27650342-830314CA-3EC6-4A7C-BA7A-8F525F65A63C

P698

Q27650342-78A05F5B-4AB3-4261-BDCC-271822C864A7

P921

Q27650342-03AFD112-AAFF-437F-90FC-BFD945AE27D9

P932

Q27650342-91007B97-1675-41D6-987C-393733434C93

P356

P1433

Journal of Biological Chemistry

P1476

Solution Structure of a Hydroc ...... erminal Domain of HIV-1 Capsid

@en

P2093

Asim K Debnath

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

Hongtao Zhang

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

Shibani Bhattacharya

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

P2860

A stapled BID BH3 helix directly binds and activates BAX

Flexibility in HIV-1 Assembly Subunits: Solution Structure of the Monomeric C-Terminal Domain of the Capsid Protein

Structure of the Antiviral Assembly Inhibitor CAP-1 Complex with the HIV-1 CA Protein

Structure of full-length HIV-1 CA: a model for the mature capsid lattice

Solution structure of a double mutant of the carboxy-terminal dimerization domain of the HIV-1 capsid protein

Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin

Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein

Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA

PRODRG: a tool for high-throughput crystallography of protein-ligand complexes

AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR

P304

16274-8

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

P31

scholarly article

P356

10.1074/JBC.C800048200

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

P407

P433

24

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

P478

283

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

P50

P577

2008-06-13T00:00:00Z

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

P698

18417468

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

P921

P932

2423268

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