Mars -- robust automatic backbone assignment of proteins.
about
OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysisNMR structure determination for larger proteins using backbone-only dataStructures of the compact helical core domains of feline calicivirus and murine norovirus VPg proteinsGANA--a genetic algorithm for NMR backbone resonance assignment.Solving nucleic acid structures by molecular replacement: examples from group II intron studiesSolution structure of the C-terminal domain of Ole e 9, a major allergen of olive pollenNMR Structure of the Amino-Terminal Domain of the Lambda Integrase Protein in Complex with DNA: Immobilization of a Flexible Tail Facilitates Beta-Sheet Recognition of the Major GrooveStructure of bacteriophage SPP1 head-to-tail connection reveals mechanism for viral DNA gatingThe structure of the dust mite allergen Der p 7 reveals similarities to innate immune proteinsStructural Basis for Homodimerization of the Src-associated during Mitosis, 68-kDa Protein (Sam68) Qua1 DomainFully automated high-quality NMR structure determination of small 2H-enriched proteinsNMR-derived Topology of a GFP-photoprotein Energy Transfer Complex1H, 13C, and 15N resonance assignment of the first PDZ domain of mouse ZO-1Two Closely Spaced Tyrosines Regulate NFAT Signaling in B Cells via Syk Association with VavPub1p C-Terminal RRM Domain Interacts with Tif4631p through a Conserved Region Neighbouring the Pab1p Binding SitePilotin-secretin recognition in the type II secretion system of Klebsiella oxytocaStructure of the Sgt2/Get5 complex provides insights into GET-mediated targeting of tail-anchored membrane proteinsThe orientation of the C-terminal domain of the Saccharomyces cerevisiae Rap1 protein is determined by its binding to DNASolution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect.Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domainFtsA forms actin-like protofilaments.Solution Structure of the Ubiquitin-associated (UBA) Domain of Human Autophagy Receptor NBR1 and Its Interaction with Ubiquitin and PolyubiquitinThermodynamic and structural investigation of the specific SDS binding ofhumicola insolenscutinaseStructure of Nipah virus unassembled nucleoprotein in complex with its viral chaperoneThe TDP-43 N-terminal domain structure at high resolutionProbabilistic interaction network of evidence algorithm and its application to complete labeling of peak lists from protein NMR spectroscopyEZ-ASSIGN, a program for exhaustive NMR chemical shift assignments of large proteins from complete or incomplete triple-resonance dataNMRFAM-SDF: a protein structure determination frameworkCapturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular ModelingModern Technologies of Solution Nuclear Magnetic Resonance Spectroscopy for Three-dimensional Structure Determination of Proteins Open Avenues for Life ScientistsA unified NMR strategy for high-throughput determination of backbone fold of small proteins.Facile backbone (1H, 15N, 13Ca, and 13C') assignment of 13C/15N-labeled proteins using orthogonal projection planes of HNN and HN(C)N experiments and its automation.Identification of a Plasmodium falciparum inhibitor-2 motif involved in the binding and regulation activity of protein phosphatase type 1RASP: rapid and robust backbone chemical shift assignments from protein structure.An automated framework for NMR resonance assignment through simultaneous slice picking and spin system forming.GASA: a graph-based automated NMR backbone resonance sequential assignment program.NVR-BIP: Nuclear Vector Replacement using Binary Integer Programming for NMR Structure-Based Assignments.Median Modified Wiener Filter for nonlinear adaptive spatial denoising of protein NMR multidimensional spectra.Structural biology by NMR: structure, dynamics, and interactions.Reliable resonance assignments of selected residues of proteins with known structure based on empirical NMR chemical shift prediction
P2860
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P2860
Mars -- robust automatic backbone assignment of proteins.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Mars -- robust automatic backbone assignment of proteins.
@en
type
label
Mars -- robust automatic backbone assignment of proteins.
@en
prefLabel
Mars -- robust automatic backbone assignment of proteins.
@en
P1476
Mars -- robust automatic backbone assignment of proteins.
@en
P2093
Markus Zweckstetter
Young-Sang Jung
P356
10.1023/B:JNMR.0000042954.99056.AD
P577
2004-09-01T00:00:00Z
P6179
1046844068