The three recombinant domains of human serum albumin. Structural characterization and ligand binding properties.
about
Crystal structural analysis of human serum albumin complexed with hemin and fatty acidVapor conjugation of toluene diisocyanate to specific lysines of human albuminHuman albumin solution for patients with cirrhosis and acute on chronic liver failure: Beyond simple volume expansionReview: modifications of human serum albumin and their binding effectUnraveling the Interaction between FcRn and Albumin: Opportunities for Design of Albumin-Based TherapeuticsSimple bioconjugate chemistry serves great clinical advances: albumin as a versatile platform for diagnosis and precision therapyStereo-selectivity of human serum albumin to enantiomeric and isoelectronic pollutants dissected by spectroscopy, calorimetry and bioinformaticsAn albumin-derived peptide scaffold capable of binding and catalysisDo hydration dynamics follow the structural perturbation during thermal denaturation of a protein: a terahertz absorption study.Emerging strategies in microbial haem capture.Effect of ibuprofen and warfarin on the allosteric properties of haem-human serum albumin. A spectroscopic study.Binding and relaxometric properties of heme complexes with cyanogen bromide fragments of human serum albumin.Characterization of the low molecular weight human serum proteome.Psoralen and coumarin photochemistry in HSA complexes and DMPC vesicles.Stereoselective binding of mexiletine and ketoprofen enantiomers with human serum albumin domainsCharacterization of the binding of sulfonylurea drugs to HSA by high-performance affinity chromatography.Biological characteristics of two lysines on human serum albumin in the high-affinity binding of 4Z,15Z-bilirubin-IXα revealed by phage display.The effects of glycation on the binding of human serum albumin to warfarin and L-tryptophan.Chromatographic analysis of acetohexamide binding to glycated human serum albuminLocating high-affinity fatty acid-binding sites on albumin by x-ray crystallography and NMR spectroscopy.Overcoming the heme paradox: heme toxicity and tolerance in bacterial pathogens.Characterization of interaction kinetics between chiral solutes and human serum albumin by using high-performance affinity chromatography and peak profilingOne ring to rule them all: trafficking of heme and heme synthesis intermediates in the metazoansDetermination of some hydrodynamic parameters of ovine serum albumin solutions using viscometric measurements.The interaction of fatty acid amide hydrolase (FAAH) inhibitors with an anandamide carrier protein using (19)F-NMR.Plasma protein homocysteinylation in uremia.Stereoselective binding of chiral drugs to plasma proteinsModeling kinetics of subcellular disposition of chemicals.Bacterial heme-transport proteins and their heme-coordination modes.Review: Glycation of human serum albumin.Fab-dsFv: A bispecific antibody format with extended serum half-life through albumin binding.Trafficking of heme and porphyrins in metazoa.Targeting the Endocannabinoid System for Neuroprotection: A (19)F-NMR Study of a Selective FAAH Inhibitor Binding with an Anandamide Carrier Protein, HSA.Time-insensitive fluorescent sensor for human serum albumin and its unusual red shiftArtificial metalloenzymes as catalysts in stereoselective Diels-Alder reactions.Structural insights into human serum albumin-mediated prostaglandin catalysis.Albumin and its application in drug delivery.Human Serum Albumin Nanoparticles for Use in Cancer Drug Delivery: Process Optimization and In Vitro Characterization.Novel role for albumin in innate immunity: serum albumin inhibits the growth of Blastomyces dermatitidis yeast form in vitroSpectroscopic studies on the interaction of a water soluble porphyrin and two drug carrier proteins.
P2860
Q21256430-E01E224F-1D66-48C6-8BAE-68EBF70C2885Q23915630-1F31CB43-08EC-47D2-B826-FFBC0EAB9ED6Q26765249-2D945C53-29B3-41C8-96B3-1A39F1902C4EQ26829605-EF879FD6-D4A1-4D58-96F8-3982C1548333Q27027238-1C17748A-1F0C-4323-B3E7-611C22010C71Q28397980-98353C5A-B88D-459E-B28C-FA840C688B26Q28477752-22EA8164-9B2C-4C08-B1C5-7F549FA3AEE8Q28486633-7DA125F7-B483-4B9D-9D34-1AAB4B8991D0Q30464627-98CDA855-BE3F-46A0-8295-A6AD98DCF81DQ30636480-8E5E7101-9F63-47DB-AEED-1197ED00CCEBQ30666587-7CA22CAE-AE8E-4E08-9C33-D79616F78719Q30731693-3357778C-2FC3-4946-9DE6-AA4F4AD22812Q31153810-3E4C4AC9-238F-49A9-8C90-820FE481D573Q33222983-3DE9F5E5-39F8-4455-AC71-AACA7CB32735Q33567391-5DAAFB14-3FA0-4D26-B47A-6A323F88AB5EQ33876316-46551A66-B109-439C-84B1-21635369413FQ34007697-F80C1B60-67E7-48EF-8F8C-5D058692D3ADQ34009043-7A99A7D2-7DBF-4D2B-81F0-5C36FF9F1B5DQ34189372-6124139A-143D-44F4-B8B7-A35F65E48EC5Q34212667-938F5FFD-1633-4611-B12A-2981D1443A17Q34309767-B408525C-D00B-4F67-A3CD-64A8951DBF62Q35212114-423D2AB2-F5AA-4E58-B8B1-4C62557BFE36Q36143730-C7C6578A-71E8-4C25-8655-D72D1ACA65F6Q36273098-9015014B-6BFD-491F-B405-2F9FB4CC2BFCQ36910533-22A8FEB8-CAFD-4142-8724-7DED13E8EFB5Q36971861-82709E75-D66B-4BD5-AA9E-7928129EA1E9Q37069257-A505DCC3-D221-423D-96AB-2530E1D9BDCAQ37194304-5662DB6A-3AE3-4E62-AE7B-78D4D6974FDFQ37195856-A4612BC2-BDA2-47DA-9098-05C5403CB26FQ37227387-3EF17E87-ADD1-4681-BDBC-218F543AD5F2Q37327316-3DF1FC21-037F-4226-9395-C2374DA42B8EQ37403265-04A96526-D4AD-41D3-9550-14DE25BC3D73Q37579319-C325F95F-A931-437B-9D2F-8165C60F7FD8Q37696951-54585CDA-F31E-4486-93A2-C322CBE0AC01Q38019867-5AFCC6DB-EDB8-4620-963B-F49D33913568Q38269100-E81BE534-229A-4095-A339-D6F94A55D9CCQ38292087-B58103B7-DA04-488A-A866-C27A85226B22Q38807982-82E62EBA-662C-4D96-AA6A-A548DC791A0DQ39982518-B503C5C2-A733-44BB-AA7E-61384F9479D5Q40203382-69F0F836-C44B-42CC-847F-7342D435B7AE
P2860
The three recombinant domains of human serum albumin. Structural characterization and ligand binding properties.
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The three recombinant domains ...... and ligand binding properties.
@ast
The three recombinant domains ...... and ligand binding properties.
@en
type
label
The three recombinant domains ...... and ligand binding properties.
@ast
The three recombinant domains ...... and ligand binding properties.
@en
prefLabel
The three recombinant domains ...... and ligand binding properties.
@ast
The three recombinant domains ...... and ligand binding properties.
@en
P2093
P2860
P356
P1476
The three recombinant domains ...... and ligand binding properties.
@en
P2093
P2860
P304
29303-29310
P356
10.1074/JBC.274.41.29303
P407
P577
1999-10-01T00:00:00Z