Ligand deconstruction: Why some fragment binding positions are conserved and others are not - Wikidata - awgldk - TriplyDB

Ligand deconstruction: Why some fragment binding positions are conserved and others are not

Ligand deconstruction: Why some fragment binding positions are conserved and others are not

http://www.wikidata.org/entity/Q35616254

about

Mycobacterium tuberculosis Malate Synthase Structures with Fragments Reveal a Portal for Substrate/Product Exchange New Frontiers in Druggability AlphaSpace: Fragment-Centric Topographical Mapping To Target Protein-Protein Interaction Interfaces.Twenty years on: the impact of fragments on drug discovery.Ligand and Target Discovery by Fragment-Based Screening in Human Cells.Lessons from Hot Spot Analysis for Fragment-Based Drug Discovery.Focused grid-based resampling for protein docking and mapping.What is the future for fragment-based drug discovery?Computational functional group mapping for drug discovery.Substrate Fragmentation for the Design of M. tuberculosis CYP121 Inhibitors.Binding Pose Flip Explained via Enthalpic and Entropic Contributions.Fragments and hot spots in drug discovery.The Ligand Binding Landscape of Diacylglycerol Kinases.Exhaustive sampling of the fragment space associated to a molecule leading to the generation of conserved fragments.When Does Chemical Elaboration Induce a Ligand To Change Its Binding Mode?Dynamic undocking and the quasi-bound state as tools for drug discovery.Label-free NMR-based dissociation kinetics determination.Fluorogenic structure activity library pinpoints molecular variations in substrate specificity of structurally homologous esterases Surface Probing by Fragment-Based Screening and Computational Methods Identifies Ligandable Pockets on the von Hippel-Lindau (VHL) E3 Ubiquitin Ligase Computational Analysis for the Rational Design of Anti-Amyloid Beta (Aβ) Antibodies

P2860

Q27728469-E63F2329-9BAB-4B6D-99CF-DC90D5C06478 Q35730955-6511D41C-9FB9-45F8-A599-93C8F3FDE97E Q35997296-8F58195C-E353-4E22-ACBD-3981E285D881 Q36078186-314CB545-7224-4E73-A637-66C20BDD5DE5 Q36256789-46581197-F3F3-4951-A289-97D1FC9F0D1A Q36269125-4164251A-964D-4F0D-BE44-DF2C9D764C7D Q36746240-3A44F8E9-5697-4663-9622-6210579086A9 Q38644516-2041B8CD-BD45-472D-979C-0E66E7B89F58 Q38890648-C3B32246-91E1-4CC2-990C-00B8F6910619 Q41109181-08144F6A-3746-48B3-A79A-67A9BA66F15F Q42319095-F416F300-A227-4159-B612-44AA5F526DCA Q42635679-53F34A9D-98EE-44D3-84FD-D1E3A064759A Q45063416-2E45A5E5-8562-4EBC-A05F-B361295AB54D Q47632897-F4F7ADA0-08F0-4ACA-8EC5-D7111C1E8C9E Q48145820-C08A91E3-7560-4EB5-80A5-CCEA274525C6 Q48213832-FEDB45B7-B46A-4A32-BDC8-C69586708BB2 Q49969718-604FDCA6-CC70-46E8-B476-4B1BDC6DDCA3 Q57159623-1A996B40-CCC1-4292-91D2-5E60AAA4A115 Q57167826-94603568-7C18-41EE-AE94-D82EB973224F Q57903229-722BB8E6-482A-4045-8E99-567746C81C7D

P2860

Ligand deconstruction: Why some fragment binding positions are conserved and others are not

http://www.wikidata.org/entity/Q35616254

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

Ligand deconstruction: Why som ...... e conserved and others are not

@ast

Ligand deconstruction: Why som ...... e conserved and others are not

@en

type

label

Ligand deconstruction: Why som ...... e conserved and others are not

@ast

Ligand deconstruction: Why som ...... e conserved and others are not

@en

prefLabel

Ligand deconstruction: Why som ...... e conserved and others are not

@ast

Ligand deconstruction: Why som ...... e conserved and others are not

@en

P1433

Q35616254-86126AF3-F974-444D-8749-B3B7CC006C40

P1476

Q35616254-8ADD8769-89B9-40E7-9B90-3C20D2E72E2D

P2093

Q35616254-0FBDCC4C-DFCD-4358-AB4D-055DC0EC59AA

Q35616254-160BC82A-CF19-43BD-9A42-716BF3B3DA27

Q35616254-46848301-A433-45EB-BBA4-491C6062CE48

Q35616254-AC4CCE10-0BB2-4C36-B166-BE0AF83D40D9

Q35616254-AF88D8AC-A42E-4368-8A14-CF4AE9533735

Q35616254-EA61807C-16E4-47FC-B83E-78D494D50D94

Q35616254-EFADC410-DD8E-45AE-A18B-3AE5F58EBE1B

Q35616254-F379BC62-07BC-4931-B9C6-236932429664

Q35616254-F4F57FC3-CF27-48BB-A87A-3E2881C34BF2

P2860

Q35616254-0511C9A2-ED95-47BF-B6A7-AF9D7F1363F4

Q35616254-058ED905-F145-4EB3-8412-1C1084A29507

Q35616254-065F079E-E9B0-43FB-BAF9-775917EA63F1

Q35616254-09DF330E-91FF-40F9-AA61-8C83DD9B159D

Q35616254-153A83B1-BD65-4AA8-B4E7-4C10A471F057

Q35616254-1673FCD2-5ACA-4CDE-9F23-030CD6130DC9

Q35616254-1985F6E4-BE29-48F2-85A7-B903F266D72B

Q35616254-2AA29C3C-B749-4228-AD17-31721F305B29

Q35616254-2B67BE34-026D-47A6-950C-7D6A8A7A2E84

Q35616254-2C5C67AB-BB93-43A7-8DAE-FCADE78BBFB1

P304

Q35616254-CE8B5F72-CB33-4028-9AA8-AF6EBA365872

P31

Q35616254-96D07738-54EA-473C-B933-545CE6618130

P356

Q35616254-9D34DE78-10C5-4ED1-8801-070BE30F5090

P407

Q35616254-39EDC7AE-06FC-4D72-B025-C037FA79C280

P433

Q35616254-DF07FF8B-A698-4DCA-A0CE-0F69553A95B0

P478

Q35616254-6210CDFA-F7AB-4C1B-9F6F-C164FD35854B

P50

Q35616254-42E8B6F4-2134-4371-BBBD-F328A5770DCB

P577

Q35616254-19C69818-910F-44B3-A7A1-794DEB38AEEE

P5875

Q35616254-E85BA121-2623-45F5-8521-609D5B740AA1

P698

Q35616254-35873839-DEAA-44D1-9169-F8E981D03DEA

P932

Q35616254-9EDD76E4-D500-4899-B346-24BA875E9B97

P356

PNAS.1501567112

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Ligand deconstruction: Why som ...... e conserved and others are not

@en

P2093

Adrian Whitty

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

David R Hall

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

Dima Kozakov

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

Elizabeth V Jones

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

Karen N Allen

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

Lingqi Luo

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

Michael Pollastri

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

Sandor Vajda

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

Stefan O Ochiana

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

P2860

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

The Protein Data Bank

Structural conservation of druggable hot spots in protein-protein interfaces

Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs

Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog

Binding of small molecules to an adaptive protein-protein interface

Structure-Guided Design and Optimization of Small Molecules Targeting the Protein–Protein Interaction between the von Hippel–Lindau (VHL) E3 Ubiquitin Ligase and the Hypoxia Inducible Factor (HIF) Alpha Subunit with in Vitro Nanomolar Affinities

Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors

Potent small-molecule binding to a dynamic hot spot on IL-2

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

P304

E2585-94

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

P31

scholarly article

P356

10.1073/PNAS.1501567112

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

P407

P433

20

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

P478

112

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

P50

P577

2015-04-27T00:00:00Z

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

P5875

275582358

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

P698

25918377

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

P932

4443342

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