Human recombinant [C22A] FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from NMR - Wikidata - awgldk - TriplyDB

Human recombinant [C22A] FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from NMR

Human recombinant [C22A] FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from NMR

http://www.wikidata.org/entity/Q36280159

about

KIT kinase mutants show unique mechanisms of drug resistance to imatinib and sunitinib in gastrointestinal stromal tumor patients Unique domain appended to vertebrate tRNA synthetase is essential for vascular development Analytical Aspects of Hydrogen Exchange Mass Spectrometry N-terminal extension changes the folding mechanism of the FK506-binding protein Inter- and intra-molecular migration of peptide amide hydrogens during electrospray ionization.Probing protein structure and dynamics by hydrogen exchange-mass spectrometry.Considerations in the analysis of hydrogen exchange mass spectrometry data.Modeling data from titration, amide H/D exchange, and mass spectrometry to obtain protein-ligand binding constants.Practical aspects of the maximum entropy inversion of the laplace transform for the quantitative analysis of multi-exponential data.The Deuterator: software for the determination of backbone amide deuterium levels from H/D exchange MS data.Chemical inhibition of prometastatic lysyl-tRNA synthetase-laminin receptor interaction.Conformational states of human purine nucleoside phosphorylase at rest, at work, and with transition state analogues Drug binding and resistance mechanism of KIT tyrosine kinase revealed by hydrogen/deuterium exchange FTICR mass spectrometry.Local conformational stability of HIV-1 gp120 in unliganded and CD4-bound states as defined by amide hydrogen/deuterium exchange Structural context for mobilization of a human tRNA synthetase from its cytoplasmic complex Epitope mapping of a 95 kDa antigen in complex with antibody by solution-phase amide backbone hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry.The N-terminal Domain of Escherichia coli Assimilatory NADPH-Sulfite Reductase Hemoprotein Is an Oligomerization Domain That Mediates Holoenzyme Assembly.Uncovering of a short internal peptide activates a tRNA synthetase procytokine.Hydrogen/deuterium exchange studies of native rabbit MM-CK dynamics Nucleotide-induced conformational changes of tetradecameric GroEL mapped by H/D exchange monitored by FT-ICR mass spectrometry Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry.DNA Interactions Probed by Hydrogen-Deuterium Exchange (HDX) Fourier Transform Ion Cyclotron Resonance Mass Spectrometry Confirm External Binding Sites on the Minichromosomal Maintenance (MCM) Helicase.Enhanced digestion efficiency, peptide ionization efficiency, and sequence resolution for protein hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry.Bottom-up hydrogen deuterium exchange mass spectrometry: data analysis and interpretation.Epitope mapping of 7S cashew antigen in complex with antibody by solution-phase H/D exchange monitored by FT-ICR mass spectrometry.Stabilization of conformationally dynamic helices by covalently attached acyl chains.The backbone dynamics of the amyloid precursor protein transmembrane helix provides a rationale for the sequential cleavage mechanism of γ-secretase.Immucillin-H binding to purine nucleoside phosphorylase reduces dynamic solvent exchange.ESI hydrogen/deuterium exchange can count chemical forms of heteroatom-bound hydrogen.Rapid screening for potential epitopes reactive with a polycolonal antibody by solution-phase H/D exchange monitored by FT-ICR mass spectrometry.Functional visualization of viral molecular motor by hydrogen-deuterium exchange reveals transient states.Improved sequence resolution by global analysis of overlapped peptides in hydrogen/deuterium exchange mass spectrometry.Automatic analysis of hydrogen/deuterium exchange mass spectra of peptides and proteins using calculations of isotopic distributions.Modeling deuterium exchange behavior of ERK2 using pepsin mapping to probe secondary structure.Mapping Residual Structure in Intrinsically Disordered Proteins at Residue Resolution Using Millisecond Hydrogen/Deuterium Exchange and Residue Averaging

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P2860

Human recombinant [C22A] FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from NMR

http://www.wikidata.org/entity/Q36280159

description

1997 nî lūn-bûn

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1997年の論文

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1997年学术文章

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1997年学术文章

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1997年学术文章

@zh-hans

1997年学术文章

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1997年学术文章

@zh-sg

1997年學術文章

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1997年學術文章

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1997年學術文章

@zh-hant

name

Human recombinant [C22A] FK506 ...... atch and extend those from NMR

@ast

Human recombinant [C22A] FK506 ...... atch and extend those from NMR

@en

type

label

Human recombinant [C22A] FK506 ...... atch and extend those from NMR

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Human recombinant [C22A] FK506 ...... atch and extend those from NMR

@en

prefLabel

Human recombinant [C22A] FK506 ...... atch and extend those from NMR

@ast

Human recombinant [C22A] FK506 ...... atch and extend those from NMR

@en

P1433

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Protein Science

P1476

Human recombinant [C22A] FK506 ...... atch and extend those from NMR

@en

P2093

A G Marshall

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

M Li

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

T M Logan

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

W Li

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

Z Zhang

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

P2860

Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex

Hydrogen exchange and structural dynamics of proteins and nucleic acids

Hydrogen exchange measurement of the free energy of structural and allosteric change in hemoglobin.

Protein hydrogen exchange studied by the fragment separation method.

Fluctuations of protein structure as expressed in the distribution of hydrogen exchange rate constants.

Mass spectrometric measurement of protein amide hydrogen exchange rates of apo- and holo-myoglobin.

Mechanisms and uses of hydrogen exchange.

Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry.

Infrared multiphoton dissociation of large multiply charged ions for biomolecule sequencing.

Detection of transient protein folding populations by mass spectrometry.

P304

2203-2217

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scholarly article

P356

10.1002/PRO.5560061015

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10

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6

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1997-10-01T00:00:00Z

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227768274

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9336843

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2143553

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