Refined apoprotein structure of rat intestinal fatty acid binding protein produced in Escherichia coli
about
Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding foldSolution structure of ileal lipid binding protein in complex with glycocholateApo-nitrophorin 4 at atomic resolutionStructure of the human-heart fatty-acid-binding protein 3 in complex with the fluorescent probe 1-anilinonaphthalene-8-sulphonic acidStructural Basis for Ligand Regulation of the Fatty Acid-binding Protein 5, Peroxisome Proliferator-activated Receptor / (FABP5-PPAR / ) Signaling PathwayProtein HP1028 from the human pathogen Helicobacter pylori belongs to the lipocalin familyThe crystal structure of the liver fatty acid-binding protein. A complex with two bound oleatesDeconstructing honeybee vitellogenin: novel 40 kDa fragment assigned to its N terminus.Local Unfolding of Fatty Acid Binding Protein to Allow Ligand Entry for Binding.Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure.Solvent-induced differentiation of protein backbone hydrogen bonds in calmodulin.Recombinant Fasciola hepatica fatty acid binding protein suppresses toll-like receptor stimulation in response to multiple bacterial ligandsMeasuring unfolding of proteins in the presence of denaturant using fluorescence correlation spectroscopy.Improved prediction of protein secondary structure by use of sequence profiles and neural networksPreparation, crystallization and preliminary X-ray diffraction analysis of two intestinal fatty-acid binding proteins in the presence of 11-(dansylamino)undecanoic acid.The integrity of the alpha-helical domain of intestinal fatty acid binding protein is essential for the collision-mediated transfer of fatty acids to phospholipid membranes.The three-dimensional structure of a helix-less variant of intestinal fatty acid-binding proteinSequence of the hexameric juvenile hormone-binding protein from the hemolymph of Locusta migratoria.Ligand Binding Induces Conformational Changes in Human Cellular Retinol-binding Protein 1 (CRBP1) Revealed by Atomic Resolution Crystal Structures.Synthesis of a gene for rat liver fatty-acid-binding protein and its expression in Escherichia coli.Identification and expression analysis of fabp2 gene from common carp Cyprinus carpio.Novel Molecular Interactions of Acylcarnitines and Fatty Acids with Myoglobin.Comparative evolutionary genomics of medaka and three-spined stickleback fabp2a and fabp2b genes with fabp2 of zebrafish.Phenylalanine side chain behavior of the intestinal fatty acid-binding protein: the effect of urea on backbone and side chain stability.The Antinociceptive Agent SBFI-26 Binds to Anandamide Transporters FABP5 and FABP7 at Two Different Sites.
P2860
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P2860
Refined apoprotein structure of rat intestinal fatty acid binding protein produced in Escherichia coli
description
1989 nî lūn-bûn
@nan
1989 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Refined apoprotein structure o ...... n produced in Escherichia coli
@ast
Refined apoprotein structure o ...... n produced in Escherichia coli
@en
Refined apoprotein structure o ...... n produced in Escherichia coli
@nl
type
label
Refined apoprotein structure o ...... n produced in Escherichia coli
@ast
Refined apoprotein structure o ...... n produced in Escherichia coli
@en
Refined apoprotein structure o ...... n produced in Escherichia coli
@nl
prefLabel
Refined apoprotein structure o ...... n produced in Escherichia coli
@ast
Refined apoprotein structure o ...... n produced in Escherichia coli
@en
Refined apoprotein structure o ...... n produced in Escherichia coli
@nl
P2860
P921
P356
P1476
Refined apoprotein structure o ...... n produced in Escherichia coli
@en
P2093
J C Sacchettini
L J Banaszak
P2860
P304
P356
10.1073/PNAS.86.20.7736
P407
P577
1989-10-01T00:00:00Z