Fast photochemical oxidation of proteins (FPOP) maps the epitope of EGFR binding to adnectin. - Wikidata - awgldk - TriplyDB

Fast photochemical oxidation of proteins (FPOP) maps the epitope of EGFR binding to adnectin.

Fast photochemical oxidation of proteins (FPOP) maps the epitope of EGFR binding to adnectin.

http://www.wikidata.org/entity/Q42090622

about

The diverse and expanding role of mass spectrometry in structural and molecular biology A Dynamic Model of pH-Induced Protein G'e Higher Order Structure Changes derived from Mass Spectrometric Analyses Divide and conquer: cleavable cross-linkers to study protein conformation and protein-protein interactions.Using hydroxyl radical footprinting to explore the free energy landscape of protein folding.Supercharging by m-NBA Improves ETD-Based Quantification of Hydroxyl Radical Protein Footprinting.Protein Footprinting Comes of Age: Mass Spectrometry for Biophysical Structure Assessment.The influence of adnectin binding on the extracellular domain of epidermal growth factor receptor.An improved fast photochemical oxidation of proteins (FPOP) platform for protein therapeutics.Probing structures of large protein complexes using zero-length cross-linking.Recent progress in protein-protein interaction study for EGFR-targeted therapeutics.Mapping the Binding Interface of VEGF and a Monoclonal Antibody Fab-1 Fragment with Fast Photochemical Oxidation of Proteins (FPOP) and Mass Spectrometry.Incorporation of a Reporter Peptide in FPOP Compensates for Adventitious Scavengers and Permits Time-Dependent Measurements.Relative Quantification of Sites of Peptide and Protein Modification Using Size Exclusion Chromatography Coupled with Electron Transfer Dissociation.Mass spectrometric characterization of protein structures and protein complexes in condensed and gas phase.Imaging short-lived reactive oxygen species (ROS) with endogenous contrast MRI.Mapping of Fab-1:VEGF Interface Using Carboxyl Group Footprinting Mass Spectrometry.Mapping the Energetic Epitope of an Antibody/Interleukin-23 Interaction with Hydrogen/Deuterium Exchange, Fast Photochemical Oxidation of Proteins Mass Spectrometry, and Alanine Shave Mutagenesis.Orthogonal Mass Spectrometry-Based Footprinting for Epitope Mapping and Structural Characterization: The IL-6 Receptor upon Binding of Protein Therapeutics.Mass Spectrometry-Based Fast Photochemical Oxidation of Proteins (FPOP) for Higher Order Structure Characterization.Localized conformational interrogation of antibody and antibody-drug conjugates by site-specific carboxyl group footprinting.

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Fast photochemical oxidation of proteins (FPOP) maps the epitope of EGFR binding to adnectin.

http://www.wikidata.org/entity/Q42090622

description

2014 nî lūn-bûn

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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

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2014年論文

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2014年论文

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2014年论文

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2014年论文

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name

Fast photochemical oxidation o ...... e of EGFR binding to adnectin.

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Fast photochemical oxidation of proteins

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type

label

Fast photochemical oxidation o ...... e of EGFR binding to adnectin.

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Fast photochemical oxidation of proteins

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prefLabel

Fast photochemical oxidation o ...... e of EGFR binding to adnectin.

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Fast photochemical oxidation of proteins

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S13361-014-0993-X

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Journal of the American Society for Mass Spectrometry

P1476

Fast photochemical oxidation o ...... e of EGFR binding to adnectin.

@en

P2093

Adrienne A Tymiak

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

Don L Rempel

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Guodong Chen

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Hui Wei

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Jingjie Mo

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Michael L Gross

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Richard Y-C Huang

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Yuetian Yan

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P2860

First-in-class, first-in-human phase I results of targeted agents: highlights of the 2008 American society of clinical oncology meeting

The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions

Statistical analysis of interface similarity in crystals of homologous proteins

Probing protein conformational changes in living cells by using designer binding proteins: application to the estrogen receptor.

A potent and highly specific FN3 monobody inhibitor of the Abl SH2 domain

Structures of adnectin/protein complexes reveal an expanded binding footprint

Crystal structure of the tenth type III cell adhesion module of human fibronectin

2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region

Cell signaling by receptor tyrosine kinases

Untangling the ErbB signalling network

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s13361-014-0993-x

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2084-2092

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scholarly article

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10.1007/S13361-014-0993-X

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12

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25

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Richard Y-C Huang

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2014-09-30T00:00:00Z

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266380383

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1013727235

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