Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin - Test2 - elhamkhani - TriplyDB

Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin

Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin

http://www.wikidata.org/entity/Q24610696

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Cholesterol loading and ultrastable protein interactions determine the level of tumor marker required for optimal isolation of cancer cells Synthetic Protein Scaffolds Based on Peptide Motifs and Cognate Adaptor Domains for Improving Metabolic Productivity Engineering of Metabolic Pathways by Artificial Enzyme Channels Superglue from bacteria: unbreakable bridges for protein nanotechnology Synthetic biology of antimicrobial discovery Force dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy.Protecting enzymatic function through directed packaging into bacterial outer membrane vesicles Plug-and-Play Pairing via Defined Divalent Streptavidins Structural Analysis and Optimization of the Covalent Association between SpyCatcher and a Peptide Tag Protein design: Past, present, and future Programmable biofilm-based materials from engineered curli nanofibres Programmable polyproteams built using twin peptide superglues A novel method for synthetic vaccine construction based on protein assembly Spontaneous Isopeptide Bond Formation as a Powerful Tool for Engineering Site-Specific Antibody-Drug Conjugates.Atomic force microscopy with sub-picoNewton force stability for biological applications.Topology Engineering of Proteins in Vivo Using Genetically Encoded, Mechanically Interlocking SpyX Modules for Enhanced Stability Synthesis and patterning of tunable multiscale materials with engineered cells.Nanoassembly routes stimulate conflicting antibody quantity and quality for transmission-blocking malaria vaccines.Synthesis of bioactive protein hydrogels by genetically encoded SpyTag-SpyCatcher chemistry.SpyAvidin hubs enable precise and ultrastable orthogonal nanoassembly.Plug-and-Display: decoration of Virus-Like Particles via isopeptide bonds for modular immunization.Bacterial superglue enables easy development of efficient virus-like particle based vaccines.Ultrastable atomic force microscopy: improved force and positional stability.A nucleotide-driven switch regulates flanking DNA length sensing by a dimeric chromatin remodeler An internal thioester in a pathogen surface protein mediates covalent host binding Engineering Streptavidin and a Streptavidin-Binding Peptide with Infinite Binding Affinity and Reversible Binding Capability: Purification of a Tagged Recombinant Protein to High Purity via Affinity-Driven Thiol Coupling Cellular Synthesis of Protein Catenanes.Multiplexed Sequence Encoding: A Framework for DNA Communication.SpyTag/SpyCatcher Cyclization Enhances the Thermostability of Firefly Luciferase.Kinetic Controlled Tag-Catcher Interactions for Directed Covalent Protein Assembly.Structure-guided SCHEMA recombination generates diverse chimeric channelrhodopsins Enhanced thermal stability of lichenase from Bacillus subtilis 168 by SpyTag/SpyCatcher-mediated spontaneous cyclization.Real-time single-molecule electronic DNA sequencing by synthesis using polymer-tagged nucleotides on a nanopore array.Design and characterization of a nanopore-coupled polymerase for single-molecule DNA sequencing by synthesis on an electrode array.Bacterial superglue generates a full-length circumsporozoite protein virus-like particle vaccine capable of inducing high and durable antibody responses.Nanomechanics of HaloTag tethers.Engineering Genetically-Encoded Mineralization and Magnetism via Directed Evolution.SpyLigase peptide-peptide ligation polymerizes affibodies to enhance magnetic cancer cell capture.Protein tango: the toolbox to capture interacting partners.SpyRing interrogation: analyzing how enzyme resilience can be achieved with phytase and distinct cyclization chemistries

P2860

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P2860

Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin

http://www.wikidata.org/entity/Q24610696

description

2012 nî lūn-bûn

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2012 թուականի Մարտին հրատարակուած գիտական յօդուած

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2012 թվականի մարտին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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name

Peptide tag forming a rapid co ...... ngineering a bacterial adhesin

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Peptide tag forming a rapid co ...... ngineering a bacterial adhesin

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Peptide tag forming a rapid co ...... ngineering a bacterial adhesin

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Peptide tag forming a rapid co ...... ngineering a bacterial adhesin

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Peptide tag forming a rapid co ...... ngineering a bacterial adhesin

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Peptide tag forming a rapid co ...... ngineering a bacterial adhesin

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Peptide tag forming a rapid co ...... ngineering a bacterial adhesin

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Peptide tag forming a rapid co ...... ngineering a bacterial adhesin

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Peptide tag forming a rapid co ...... ngineering a bacterial adhesin

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P1433

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PNAS.1115485109

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

P1476

Peptide tag forming a rapid co ...... ngineering a bacterial adhesin

@en

P2093

Emily C Chittock

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

Emrah Celik

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

Jacob O Fierer

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

Mark Howarth

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

Vincent T Moy

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

P2860

Total chemical synthesis of proteins

The Scottish Structural Proteomics Facility: targets, methods and outputs

A streptavidin variant with slower biotin dissociation and increased mechanostability

A fluorophore ligase for site-specific protein labeling inside living cells

The FbaB-type fibronectin-binding protein of Streptococcus pyogenes promotes specific invasion into endothelial cells.

Improved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding site

Stabilizing isopeptide bonds revealed in gram-positive bacterial pilus structure

Global analysis of protein localization in budding yeast.

Structural Basis for Exquisite Specificity of Affinity Clamps, Synthetic Binding Proteins Generated through Directed Domain-interface Evolution

Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells

P304

E690-7

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scholarly article

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2061176

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10.1073/PNAS.1115485109

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P433

12

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109

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Uli Schwarz-Linek

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2012-02-24T00:00:00Z

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221862625

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22366317

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3311370

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