Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry. - Wikidata - awgldk - TriplyDB

Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry.

Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry.

http://www.wikidata.org/entity/Q37621068

about

Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle ECL: an exhaustive search tool for the identification of cross-linked peptides using whole database Probing native protein structures by chemical cross-linking, mass spectrometry, and bioinformatics.Xlink-identifier: an automated data analysis platform for confident identifications of chemically cross-linked peptides using tandem mass spectrometry Integrating mass spectrometry of intact protein complexes into structural proteomics Protein interactions, post-translational modifications and topologies in human cells.Identification and characterization of p63 (CKAP4/ERGIC-63/CLIMP-63), a surfactant protein A binding protein, on type II pneumocytes.Interface analysis of the complex between ERK2 and PTP-SL Finding chimeras: a bioinformatics strategy for identification of cross-linked peptides.Topographic studies of the GroEL-GroES chaperonin complex by chemical cross-linking using diformyl ethynylbenzene: the power of high resolution electron transfer dissociation for determination of both peptide sequences and their attachment sites A dynamic cpSRP43-Albino3 interaction mediates translocase regulation of chloroplast signal recognition particle (cpSRP)-targeting components.The beginning of a beautiful friendship: cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes Molecular architecture of photoreceptor phosphodiesterase elucidated by chemical cross-linking and integrative modeling Conformational States of macromolecular assemblies explored by integrative structure calculation.Selective enrichment and identification of azide-tagged cross-linked peptides using chemical ligation and mass spectrometry.The structure of Escherichia coli signal recognition particle revealed by scanning transmission electron microscopy.Subunit order of eukaryotic TRiC/CCT chaperonin by cross-linking, mass spectrometry, and combinatorial homology modeling.Elucidating the higher-order structure of biopolymers by structural probing and mass spectrometry: MS3D The integrin Mac-1 (CR3) mediates internalization and directs Bacillus anthracis spores into professional phagocytes.Mapping the structural topology of the yeast 19S proteasomal regulatory particle using chemical cross-linking and probabilistic modeling.Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.Biochemical and biological functions of docosahexaenoic acid in the nervous system: modulation by ethanol SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone.Bioinformatics tools for the structural elucidation of multi-subunit protein complexes by mass spectrometric analysis of protein-protein cross-links.Chemical crosslinkers enhance detection of receptor interactomes.Change in the Molecular Dimension of a RAGE-Ligand Complex Triggers RAGE Signaling.Domain rearrangement of SRP protein Ffh upon binding 4.5S RNA and the SRP receptor FtsY Novel octavalent cross-linker displays efficient trapping of protein-protein interactions.Probing the conformation of the ISWI ATPase domain with genetically encoded photoreactive crosslinkers and mass spectrometry.Protein-protein interactions as a tool for site-specific labeling of proteins.Influence of crosslinker identity and position on gas-phase dissociation of Lys-Lys crosslinked peptides.Co-evolution of Two GTPases Enables Efficient Protein Targeting in an RNA-less Chloroplast Signal Recognition Particle Pathway.RNA-mediated interaction between the peptide-binding and GTPase domains of the signal recognition particle.Impact of proline and aspartic acid residues on the dissociation of intermolecularly crosslinked peptides.Interdomain conformational changes in Akt activation revealed by chemical cross-linking and tandem mass spectrometry.On the use of distance constraints in protein-protein docking computations.The Bacterial SRP Receptor, SecA and the Ribosome Use Overlapping Binding Sites on the SecY Translocon

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Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry.

http://www.wikidata.org/entity/Q37621068

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年學術文章

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2004年學術文章

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2004年學術文章

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name

Unraveling the interface of si ...... and tandem mass spectrometry.

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Unraveling the interface of si ...... and tandem mass spectrometry.

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type

label

Unraveling the interface of si ...... and tandem mass spectrometry.

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Unraveling the interface of si ...... and tandem mass spectrometry.

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Unraveling the interface of si ...... and tandem mass spectrometry.

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Unraveling the interface of si ...... and tandem mass spectrometry.

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PNAS.0407456101

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

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Unraveling the interface of si ...... and tandem mass spectrometry.

@en

P2093

Demetri T Moustakas

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

Feixia Chu

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Frank Alber

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Pascal F Egea

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Robert M Stroud

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Shu-ou Shan

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P2860

The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity

GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation

Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle

DOCK 4.0: Search strategies for automated molecular docking of flexible molecule databases

Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP

Crystal structure of the ribonucleoprotein core of the signal recognition particle

The crystal structure of the conserved GTPase of SRP54 from the archaeon Acidianus ambivalens and its comparison with related structures suggests a model for the SRP-SRP receptor complex

The conformation of bound GMPPNP suggests a mechanism for gating the active site of the SRP GTPase

Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication

Substrate twinning activates the signal recognition particle and its receptor

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16454-16459

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Alma L Burlingame

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2004-11-16T00:00:00Z

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8180102

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15546976

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528904

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