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56 results for “serum albumin”
Serum albumin domain structures in human blood serum by mass spectrometry and computational biology
<p>Contact prediction data generated by EPC-map used in the paper "Serum Albumin Domain Structures in Human Blood Serum by Mass Spectrometry and Computational Biology" by Rappsilber et al.</p>
Binding constants of clinical drugs and other organic ligands with human and mammalian serum albumins
<p>The dataset contains literature values of the experimental equilibrium binding constants of drugs and some other organic ligands with human and mammalian (predominantly bovine) serum albumins. There are 1755 records gathered from 346 original literature sources describing the albumin affinity of 324 different substances. The data were extracted from both articles and existing protein binding databases applying strict data selection rules in order to exclude the values influenced by the third-party compounds. For each experiment with a particular ligand–albumin system found in literature we provide (if possible) the following details: albumin source organism, ligand chemical name, canonical SMILES, InChIKey, the binding (either association <em>K<sub>a</sub></em> or dissociation <em>K<sub>d</sub></em>) constant value in molarity-based scale, temperature in K, albumin and ligand concentrations, buffer pH, composition, and concentration, experimental method, model used for the binding constant calculation, DOI or link to the source paper. For the results obtained using independent binding sites model, the average number of binding sites <em>n</em> is also provided. If two different types of binding sites were suggested, we put the second site-specific binding constant <em>K<sub>a2</sub></em> or <em>K<sub>d2</sub></em> and the number of the second-type sites<em> </em> <em>n</em><sub>2</sub> into separate columns. For some systems, the enthalpies of binding have also been determined either from the temperature dependence of the binding constant or using direct calorimetric measurements. Their values are also given in the respective column. The dataset can be used as the reference one, for the development of predictive models to calculate the binding constants, and for the choice of the experimental setup in the future albumin binding studies.</p>
Neonicotinoid trapping by the FA1 site of human serum albumin
<p><strong>Leboffe_et_al_docking_simulations:</strong> Input and output files derived from the docking simulations described in the manuscript "Neonicotinoid trapping by the FA1 site of human serum albumin" by Leboffe et al. More informations are given in the "README.txt" file.</p>
Human Serum Albumin Adductome as an Instant Dosimeter of the Potential Internal Exposure of PM2 .5
<p>This dataset contains observations and indicators for PM2.5 potential internal exposure (PIE) evaluation. The dataset including three csv files:</p> <ol> <li> Surface Plasmon Resonance (SPR) technology monitoring data of human serun albumin (HSA) -water soluble organic molecule( WSOM) interaction</li> <li>HSA-WSOM adductome abundance</li> <li>ADMET evaluation for major contributors</li> </ol> <p> </p> <p> </p>
Effect of Velphoro on Serum Phosphate and Albumin in Peritoneal Dialysis Patients
ClinicalTrials.gov study NCT04046263. IPD Sharing: YES. Countries: 1. Publications: 1.
Far-red pentamethine cyanine dyes as fluorescent probes for detection of serum albumins
<p><span>Benzothiazole based cyanine dyes with bridged groups in pentamethine chain were studied as potential far-red fluorescent probes for protein detection. Spectral-luminescent properties were characterized for unbound dyes and in the presence of serum albumins (bovine (BSA), human (HSA), equine (ESA)), and globular proteins (β-lactoglobulin, ovalbumin). We have observed that the addition of albumins leads to a significant increase in dyes fluorescence intensity. However, the fluorescent response of dyes in the presence of other globular proteins was noticeably lower. The value of fluorescence quantum yield for dye bearing sulfonate group complexed with HSA amounted to 42% compared with 0.2 % for the free dye. The detection limit of HSA by this dye was about > 0.003 mg/ml that indicates the high sensitivity of dye to low HSA concentrations. Modeling of structure of the dyes complexes with albumin molecules was performed by molecular docking. According to these data, dyes could bind to up to five sites on the HSA molecule; the most preferable are the hemin-binding site in subdomain IB and <span>the dye-binding site in the pocket between subdomains IA, IIA, and IIIA.</span> This work confirms that pentamethine cyanine dyes could be proposed as powerful far-red fluorescent probes applicable for highly sensitive detection of albumins.</span></p>
Data from: A cross-sectional study investigating the relationship between pit recovery time and serum albumin levels in bilateral lower extremity pitting oedema
<p><span><strong>Objectives</strong>:</span><span> In this study, we re-evaluated the relationship between pit recovery time (PRT) and serum albumin levels and elucidated the factors influencing PRT. </span></p> <p><span><strong>Design</strong>:</span><span> Cross-sectional study.</span></p> <p><span><strong>Setting</strong>:</span><span> Patients who visited the outpatient department or were admitted to a small urban hospital in Japan.</span></p> <p><span><strong>Participants</strong>:</span><span> 135 adult Japanese patients</span> <span>with bilateral lower extremity pitting oedema.</span></p> <p><span><strong>Interventions</strong>: </span></p> <p><strong><span>Primary and secondary outcome measures</span></strong><span>: This study assessed the correlation between PRT and serum albumin levels, calculated the predictive accuracy for identifying a group with low albumin levels when the PRT of the lower leg was < 40 s, and identified variables that influence PRT.</span></p> <p><span><strong>Results</strong>:</span><span> We found no significant correlation between lower leg PRT and serum albumin levels. Furthermore, a PRT of < 40 s was largely ineffective in predicting low albumin levels. Factors influencing PRT included the diagnosis of malnutrition oedema, examinations conducted during hospitalisation, diagnosis of cardiac oedema, use of diuretics, thickness of the lower limb soft tissue, serum creatinine level, estimated right ventricular systolic pressure (RVSP), age, serum albumin level, potassium level, and blood urea nitrogen to serum creatinine ratio. Notable correlations with PRT were observed in relation to lower limb soft tissue thickness, age, and estimated RVSP.</span></p> <p><span><strong>Conclusions</strong>:</span><span> Given that the PRT is influenced by multiple factors, its correlation with serum albumin levels is weak. Thus, predicting hypoalbuminaemia based solely on PRT is inaccurate.</span></p>
Impact of Preoperative Serum Albumin Level on Postoperative Outcomes in Chinese HCC Patients Treated With Surgery
ClinicalTrials.gov study NCT05970159. IPD Sharing: NO. Countries: 1. Publications: 2.
Effect of Non-Surgical Periodontal Therapy on Serum Albumin Levels of Patients on Maintenance Hemodialysis Therapy,
ClinicalTrials.gov study NCT01641757. IPD Sharing: Not stated. Countries: 1. Publications: 1.
Serum Albumin in Acute Coronary Syndrome
ClinicalTrials.gov study NCT06727084. IPD Sharing: NO. Countries: 1. Publications: 4.
Effects on Plasma Exchange on Functional Capacity of Serum Albumin, Circulatory Dysfunction, Renal and Cerebral Function in Cirrhotic Patients With "Acute-on-chronic Liver Failure"
ClinicalTrials.gov study NCT01201720. IPD Sharing: Not stated. Countries: 1. Publications: 1.
Prediction of Preterm Delivery by Serum Ischemia Modified Albumin, Biglycan and Decorin Levels in Women With Threatened Preterm Labour
ClinicalTrials.gov study NCT04451928. IPD Sharing: NO. Countries: 1. Publications: 3.
Serum-Ascites Albumin Gradient Analysis in Cancer Patients in Palliative Care
ClinicalTrials.gov study NCT03463655. IPD Sharing: NO. Countries: 1. Publications: 2.
Data from: A cross-sectional study investigating the relationship between pit recovery time and serum albumin levels in bilateral lower extremity pitting oedema
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Data from: Prognostic significance of serum albumin in patients with stable coronary artery disease treated by percutaneous coronary intervention
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Far-red pentamethine cyanine dyes as fluorescent probes for detection of serum albumins
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Bovine Serum Albumin (BSA)/Polyacrylonitrile (PAN) Biohybrid Nanofibers Coated with a Biomineralized Calcium Deficient Hydroxyapatite (HA) Shell for Wound Dressing
<p>Here, for the first time, a nanofibrous (NF) wound dressing is developed based on biomineralized polyacrylonitrile<br> (PAN) nanofibers. In contrast to the majority of the currently available nanofibrous wound dressings that are based on<br> natural polymers, PAN employed in this study is a synthetic, industrial polymer that has rarely been considered for this<br> purpose. PAN NFs are first hydrolyzed to allow for tethering of biofunctional agents (here Bovine Serum Albumin<br> (BSA)). Later, the biofunctionlized PAN NFs are induced to biomineralize by immersion in simulated body fluid (SBF).<br> As a result, core-shell, calcium deficient hydroxyapatite (HA)/BSA/PAN nanofibers form, that are larger in<br> diameter (318 vs. 298 nm) and mechanically stronger (elastic modulus; 8.5 vs. 6 MPa) compared to the untreated PAN<br> NFs. The biomineralized PAN NFs showed promising bioactivity as reflected in the cell biology tests with fibroblast and<br> keratinocyte cells. Hs68 fibroblasts and HaCat keratinocytes were found to be more viable in the presence of the<br> biomineralized NFs than when they were co-cultured with the neat PAN NFs. Such mechanical and biological<br> characteristics of the novel PAN NFs are favorable for wound dressing applications. More importantly, given the simple<br> and cost-effective surface treatment approach presented here and the widely available knowledge for large scale,<br> industrial processing of PAN, the present nanofibrous material holds promise for medical translation and further<br> investigations leading to commercialization strategies.</p>
Data from: Identification and mapping of linear antibody epitopes in human serum albumin using high-density peptide arrays
We have recently developed a high-density photolithographic, peptide array technology with a theoretical upper limit of 2 million different peptides per array of 2 cm2. Here, we have used this to perform complete and exhaustive analyses of linear B cell epitopes of a medium sized protein target using human serum albumin (HSA) as an example. All possible overlapping 15-mers from HSA were synthesized and probed with a commercially available polyclonal rabbit anti-HSA antibody preparation. To allow for identification of even the weakest epitopes and at the same time perform a detailed characterization of key residues involved in antibody binding, the array also included complete single substitution scans (i.e. including each of the 20 common amino acids) at each position of each 15-mer peptide. As specificity controls, all possible 15-mer peptides from bovine serum albumin (BSA) and from rabbit serum albumin (RSA) were included as well. The resulting layout contained more than 200.000 peptide fields and could be synthesized in a single array on a microscope slide. More than 20 linear epitope candidates were identified and characterized at high resolution i.e. identifying which amino acids in which positions were needed, or not needed, for antibody interaction. As expected, moderate cross-reaction with some peptides in BSA was identified whereas no cross-reaction was observed with peptides from RSA. We conclude that high-density peptide microarrays are a very powerful methodology to identify and characterize linear antibody epitopes, and should advance detailed description of individual specificities at the single antibody level as well as serologic analysis at the proteome-wide level.
Figure 2 from: Abarova S, Stoitchkova K, Tzonev S, Argirova M, Yancheva D, Anastassova N, Tenchov B (2024) Spectroscopic and thermodynamic characterization of the interaction of a new synthesized antitumor drug candidate 2H4MBBH with human serum albumin. Pharmacia 71: 1-5. https://doi.org/10.3897/pharmacia.71.e112385
Figure 2 Fluorescence titration curve of HSA (4 µM) with the 2H4MBBH in saline at 15 °C and 25 °C. Different curves correspond to 2H4MBBH concentrations of 0, 10, 20, 30, 40, 50 µM, respectively.
Figure 3 from: Abarova S, Stoitchkova K, Tzonev S, Argirova M, Yancheva D, Anastassova N, Tenchov B (2024) Spectroscopic and thermodynamic characterization of the interaction of a new synthesized antitumor drug candidate 2H4MBBH with human serum albumin. Pharmacia 71: 1-5. https://doi.org/10.3897/pharmacia.71.e112385
Figure 3 Stern-Volmer plots for quenching of different 2H4MBBH concentrations (10–50 µM) to HSA (4 µM) in saline at 15 and 25 °C.
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