The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ) - Wikidata - awgldk - TriplyDB

The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)

The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)

http://www.wikidata.org/entity/Q27618002

about

S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo Structural and functional insights into RAGE activation by multimeric S100B Solution structure of DinI provides insight into its mode of RecA inactivation Expanding the utility of NMR restraints with paramagnetic compounds: background and practical aspects The Effects of CapZ Peptide (TRTK-12) Binding to S100B–Ca2+ as Examined by NMR and X-ray Crystallography Restriction Endonuclease Inhibitor IPI* of Bacteriophage T4: A Novel Structure for a Dedicated Target Analysis of the structure of human apo-S100B at low temperature indicates a unimodal conformational distribution is adopted by calcium-free S100 proteins S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor Refinement of the solution structure and dynamic properties of Ca2+-bound rat S100B The 1.5 A Crystal Structure of Human Receptor for Advanced Glycation Endproducts (RAGE) Ectodomains Reveals Unique Features Determining Ligand Binding Post-translational S-Nitrosylation Is an Endogenous Factor Fine Tuning the Properties of Human S100A1 Protein Structure of the Small Dictyostelium discoideum Myosin Light Chain MlcB Provides Insights into MyoB IQ Motif Recognition An Interplay of S-Nitrosylation and Metal Ion Binding for Astrocytic S100B Protein Weak alignment offers new NMR opportunities to study protein structure and dynamics.Protein structure prediction using sparse dipolar coupling data.Rapid protein fold determination using unassigned NMR data.Molecular dynamics simulation of S100B protein to explore ligand blockage of the interaction with p53 protein.Diversity of conformational states and changes within the EF-hand protein superfamily.Structural changes in the C-terminus of Ca2+-bound rat S100B (beta beta) upon binding to a peptide derived from the C-terminal regulatory domain of p53.Calcium-dependent and -independent interactions of the S100 protein family.Solution structure of (gamma)S-crystallin by molecular fragment replacement NMR.S100-annexin complexes--structural insights.Improvement and analysis of computational methods for prediction of residual dipolar couplings Solution structure and backbone dynamics of Calsensin, an invertebrate neuronal calcium-binding protein.Calretinin and calbindin D28k have different domain organizations.The Calcium-Dependent Interaction of S100B with Its Protein Targets.Estimating the accuracy of protein structures using residual dipolar couplings.

P2860

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P2860

The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)

http://www.wikidata.org/entity/Q27618002

description

1999 nî lūn-bûn

@nan

1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի ապրիլին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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name

The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)

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The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)

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The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)

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The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)

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The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)

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The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)

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The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)

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The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)

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The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)

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The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)

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A C Drohat

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

D J Weber

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D M Baldisseri

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N Tjandra

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P2860

A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form

The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine. Molecular details, ion binding, and implications for the structure of other calcium-binding proteins

The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins

Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy

The solution structure of the bovine S100B protein dimer in the calcium-free state

Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution

Solution structure of calcium-bound rat S100B(betabeta) as determined by nuclear magnetic resonance spectroscopy,

The three-dimensional structure of Ca(2+)-bound calcyclin: implications for Ca(2+)-signal transduction by S100 proteins

A novel mode of target recognition suggested by the 2.0 A structure of holo S100B from bovine brain

Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions

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1780540

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10.1110/PS.8.4.800

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10211826

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