Enhancement of α-Helix Mimicry by an α/β-Peptide Foldamer via Incorporation of a Dense Ionic Side-Chain Array - sprookjes - yvandenbroek - TriplyDB

Enhancement of α-Helix Mimicry by an α/β-Peptide Foldamer via Incorporation of a Dense Ionic Side-Chain Array

Enhancement of α-Helix Mimicry by an α/β-Peptide Foldamer via Incorporation of a Dense Ionic Side-Chain Array

http://www.wikidata.org/entity/Q27678660

about

Multi-Facial, Non-Peptidic α-Helix Mimetics Differential Impact of β and γ Residue Preorganization on α/β/γ-Peptide Helix Stability in Water A potent α/β-peptide analogue of GLP-1 with prolonged action in vivo.Folding and function in α/β-peptides: targets and therapeutic applications.Computer-Aided Approaches for Targeting HIVgp41.Cell death and the mitochondria: therapeutic targeting of the BCL-2 family-driven pathway.Residue-Based Preorganization of BH3-Derived α/β-Peptides: Modulating Affinity, Selectivity and Proteolytic Susceptibility in α-Helix Mimics.Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes.Targeting recognition surfaces on natural proteins with peptidic foldamers Iterative Nonproteinogenic Residue Incorporation Yields α/β-Peptides with a Helix-Loop-Helix Tertiary Structure and High Affinity for VEGF.Induced folding of protein-sized foldameric β-sandwich models with core β-amino acid residues.Orthogonal functionalisation of α-helix mimetics Positive allostery in metal ion binding by a cooperatively folded β-peptide bundle.α-Helix mimicry with α/β-peptides.Backbone Modification of a Parathyroid Hormone Receptor-1 Antagonist/Inverse Agonist Formation of a pseudo-β-hairpin motif utilizing the Ant-Pro reverse turn: consequences of stereochemical reordering.The Exonization and Functionalization of an Alu-J Element in the Protein Coding Region of Glycoprotein Hormone Alpha Gene Represent a Novel Mechanism to the Evolution of Hemochorial Placentation in Primates.Evaluation of β-Amino Acid Replacements in Protein Loops: Effects on Conformational Stability and Structure.Development of Potent, Protease-Resistant Agonists of the Parathyroid Hormone Receptor with Broad β Residue Distribution.Impact of Backbone Pattern and Residue Substitution on Helicity in α/β/γ-Peptides.A modular synthesis of teraryl-based α-helix mimetics, part 1: Synthesis of core fragments with two electronically differentiated leaving groups.

P2860

Q26781261-7C423CC8-79E5-480D-B02D-902A52EB03C2 Q27678274-CFFF2C2F-7EBA-49B5-A4E0-BFF2E24FB218 Q34282783-83486676-DD6C-485A-9601-9A87FE9D7AF1 Q34483276-1E52318D-A1BE-4C55-82E6-D48577E47A83 Q38111393-BFEBDA70-B94C-423A-B714-92CB14F0358D Q38151753-C25E7366-628E-4852-B5D4-B1DA657A9B43 Q38253734-D7C3C6B3-17FB-4E00-B6F3-A4AAC299762C Q38539666-C03C47A4-1583-43C6-A9F0-20FFBD16B7FE Q38889986-CD7E7649-DFD7-43F0-BABC-6297646644F4 Q39145905-604C5053-71A8-4FC8-AE2C-1BC67AC2C483 Q41442763-F6A9A6A7-12A7-4522-8D48-9C433768D6AA Q41849399-0C5C7DCE-E773-400A-B1C1-E1EBED2D55E7 Q41888968-C4938CF7-2C53-40B6-BF24-C9614FA4957F Q41965412-DE54BB2F-2DFD-477D-A78C-DEF51A3BBE43 Q42369377-CC088A26-76FD-411A-ACE0-4D62A28B18BD Q43732823-4B7B8315-0FDD-47B6-A9F2-1BFFCEC7E239 Q46286556-E1CBF9A7-12D4-4FC8-ABC7-BA54DB7D350A Q47260358-BF57C682-F993-44F1-B3E3-222359160998 Q47416630-464C142E-51B6-4406-8B4B-1260189F8AC6 Q48210524-345467EE-E404-4DAD-AE32-2BE9810F03D6 Q51839442-F18C2F45-2F8F-44A6-809D-ED63B4AA00CB

P2860

Enhancement of α-Helix Mimicry by an α/β-Peptide Foldamer via Incorporation of a Dense Ionic Side-Chain Array

http://www.wikidata.org/entity/Q27678660

description

2012 nî lūn-bûn

@nan

2012 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Enhancement of α-Helix Mimicry ...... a Dense Ionic Side-Chain Array

@ast

Enhancement of α-Helix Mimicry ...... a Dense Ionic Side-Chain Array

@en

Enhancement of α-Helix Mimicry ...... a Dense Ionic Side-Chain Array

@nl

type

label

Enhancement of α-Helix Mimicry ...... a Dense Ionic Side-Chain Array

@ast

Enhancement of α-Helix Mimicry ...... a Dense Ionic Side-Chain Array

@en

Enhancement of α-Helix Mimicry ...... a Dense Ionic Side-Chain Array

@nl

prefLabel

Enhancement of α-Helix Mimicry ...... a Dense Ionic Side-Chain Array

@ast

Enhancement of α-Helix Mimicry ...... a Dense Ionic Side-Chain Array

@en

Enhancement of α-Helix Mimicry ...... a Dense Ionic Side-Chain Array

@nl

P1433

Q27678660-200112AD-133D-4289-8A6F-402919366520

P1476

Q27678660-C1E85199-CCDA-4FB8-854F-72C58AD1DB9A

P2093

Q27678660-0F343646-36BB-4D62-8495-6C73E96D6859

Q27678660-447003F2-D9FD-46B9-8C60-5309956A02B6

Q27678660-52C0BD72-CD1E-469E-86C7-2655E0D37D17

Q27678660-977E4CCF-A4AE-44A1-92BC-32DE7F657C68

Q27678660-DD50E62E-B16C-4B0B-A86C-815164DA0AE8

Q27678660-E1A35A8E-6E4D-4B77-B3F5-8C04F108C624

Q27678660-EC008FD1-F3C5-4E35-B61C-D432D373421D

Q27678660-F27C1F14-F5AF-455D-AEB5-EC5739FE1260

P2860

Q27678660-01241DCB-7A75-41D5-BD96-249BB98A52D9

Q27678660-046F6FE1-BA55-4F97-86FB-B4B5CF54D386

Q27678660-0AFD500D-6A85-4CB6-A0C8-6DD977EB6A06

Q27678660-0CB63112-9055-4906-A712-2E080CF1C9F9

Q27678660-1F0A92AE-4246-4D41-AC33-09930B7B3009

Q27678660-276D80BA-A5CC-4FDF-978F-D2075E84E1CF

Q27678660-330925AB-5BD6-4085-8863-5A3E5E7C3B54

Q27678660-37AE19D0-4F9A-4E83-86A7-694BEAD29754

Q27678660-389EA02C-05FF-4F18-8C9B-5371774F913A

Q27678660-394AC187-BBC2-45C1-A9F2-500BC526931D

P304

Q27678660-5CB3F9B6-3C89-4F5F-B7BB-99FB70476282

P31

Q27678660-4C17BE97-483C-48FE-A45D-89A1283AEE80

P356

Q27678660-9F163B2A-3E78-4024-B55E-159142026670

P407

Q27678660-7693C066-1403-49CB-87E7-E85A3BB664EF

P433

Q27678660-2B0B3945-D90E-474C-8553-49421EB2FCBB

P478

Q27678660-B3FB85B3-D754-462B-BB0D-0C6E2899B49F

P577

Q27678660-2AA8BE99-8C3B-45FB-98CA-4A8DFCF3CA9E

P5875

Q27678660-71A16EE4-416A-47F8-BA8C-45702440A8E3

P698

Q27678660-00F9E13A-5D61-4EF4-BE18-FF949026B338

P921

Q27678660-FD090EE9-2B19-4B9E-B9AE-1D85BE82F12E

P932

Q27678660-EFB0C167-E2EB-4ADF-9429-FDAACF28C45D

P356

P1433

Journal of the American Chemical Society

P1476

Enhancement of α-Helix Mimicry ...... a Dense Ionic Side-Chain Array

@en

P2093

David E Mortenson

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

Hyun Gi Yun

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

John P Moore

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

Lisa M Johnson

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

Min Lu

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

Samuel H Gellman

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

Thomas J Ketas

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

W Seth Horne

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

P2860

Systematic analysis of helical protein interfaces reveals targets for synthetic inhibitors

Helix bundle quaternary structure from alpha/beta-peptide foldamers

Interplay among side chain sequence, backbone composition, and residue rigidification in polypeptide folding and assembly

Structural and biological mimicry of protein surface recognition by / -peptide foldamers

Structural Consequences of β-Amino Acid Preorganization in a Self-Assembling α/β-Peptide: Fundamental Studies of Foldameric Helix Bundles

Broad Distribution of Energetically Important Contacts across an Extended Protein Interface

Structural Basis of Bcl-xL Recognition by a BH3-Mimetic α/β-Peptide Generated by Sequence-Based Design

Evaluation of Diverse α/β-Backbone Patterns for Functional α-Helix Mimicry: Analogues of the Bim BH3 Domain

Core structure of gp41 from the HIV envelope glycoprotein

Atomic structure of the ectodomain from HIV-1 gp41

P304

7317-20

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

P31

scholarly article

P356

10.1021/JA302428D

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

P407

P433

17

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

P478

134

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

P577

2012-05-02T00:00:00Z

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

P5875

224823304

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

P698

22524614

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

P921

P932

3377471

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