Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity. - Test2 - elhamkhani - TriplyDB

Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity.

Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity.

http://www.wikidata.org/entity/Q34060919

about

Genetically modified proteins: functional improvement and chimeragenesis Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli.Total chemical synthesis, refolding, and crystallographic structure of fully active immunophilin calstabin 2 (FKBP12.6)A thermostable d-polymerase for mirror-image PCR.Expanding the chemical toolbox for the synthesis of large and uniquely modified proteins.Chemical Synthesis and Characterization of an Equinatoxin II(1-85) Analogue.A synthetic molecular system capable of mirror-image genetic replication and transcription.Screening of a virtual mirror-image library of natural products.High-resolution structures of a heterochiral coiled coil An L-RNA Aptamer that Binds and Inhibits RNase.Total chemical synthesis of a thermostable enzyme capable of polymerase chain reaction All about that Amide Bond: The Sixth Chemical Protein Synthesis (CPS) Meeting.Pushing the Boundaries of Chemical Protein Synthesis: The Case of Ubiquitin Chains and Polyubiquitinated Peptides and Proteins.Chiral recognition in amyloid fiber growth.Convergent versus sequential protein synthesis: the case of ubiquitinated and glycosylated H2B.Aligator: A computational tool for optimizing total chemical synthesis of large proteins.A Helping Hand to Overcome Solubility Challenges in Chemical Protein Synthesis.Design and characterization of ebolavirus GP prehairpin intermediate mimics as drug targets.Total chemical synthesis of the site-selective azide-labeled [I66A]HIV-1 protease.Synthesis of tumor necrosis factor α for use as a mirror-image phage display target Mirror-image polymerase chain reaction.A computational approach for designing D-proteins with non-canonical amino acid optimised binding affinity.Selenium and Selenocysteine in Protein Chemistry.Method to generate highly stable D-amino acid analogs of bioactive helical peptides using a mirror image of the entire PDB.Protein chemical synthesis by α-ketoacid-hydroxylamine ligation.Total synthesis and biochemical characterization of mirror image barnase.N-Linked Glycosyl Auxiliary-Mediated Native Chemical Ligation on Aspartic Acid: Application towards N-Glycopeptide Synthesis.Synthesis of l- and d-Ubiquitin by One-Pot Ligation and Metal-Free Desulfurization.Accelerated Fmoc solid-phase synthesis of peptides with aggregation-disrupting backbones.Efficient Palladium-Assisted One-Pot Deprotection of (Acetamidomethyl)Cysteine Following Native Chemical Ligation and/or Desulfurization To Expedite Chemical Protein Synthesis.Blocking of the PD-1/PD-L1 Interaction by a D-Peptide Antagonist for Cancer Immunotherapy.

P2860

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P2860

Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity.

http://www.wikidata.org/entity/Q34060919

description

2014 nî lūn-bûn

@nan

2014 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի հուլիսին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity.

@ast

Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity.

@en

Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity.

@nl

type

label

Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity.

@ast

Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity.

@en

Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity.

@nl

prefLabel

Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity.

@ast

Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity.

@en

Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity.

@nl

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PNAS.1410900111

P1433

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

P1476

Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity.

@en

P2093

Matthew T Weinstock

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

Michael S Kay

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

Michael T Jacobsen

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

P2860

Total chemical synthesis of proteins

Potent D-peptide inhibitors of HIV-1 entry

Protease-resistant peptide design-empowering nature's fragile warriors against HIV

The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity

Convergent chemical synthesis and crystal structure of a 203 amino acid "covalent dimer" HIV-1 protease enzyme molecule

A Left-Handed Solution to Peptide Inhibition of the p53-MDM2 Interaction

Design of a Potent D-Peptide HIV-1 Entry Inhibitor with a Strong Barrier to Resistance

Chemical synthesis and X-ray structure of a heterochiral {D-protein antagonist plus vascular endothelial growth factor} protein complex by racemic crystallography

GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding

The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution

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11679-11684

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scholarly article

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10.1073/PNAS.1410900111

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32

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111

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2014-07-28T00:00:00Z

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264394188

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25071217

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molecular chaperones

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4136631

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