搜索结果: 1-15 共查到“生物化学 human”相关记录33条 . 查询时间(0.156 秒)
中国科学院动物研究所专利：MONOCLONAL ANTIBODY AGAINST HUMAN PRPC AND USE THEREOF
中国科学院动物研究所 专利 人PrPC蛋白 单克隆抗体
2024/5/31
一种抗人PrPC蛋白的单克隆抗体，能够以靶向方式降低转录因子Twist1的表达水平，并诱导巨噬细胞和NK细胞靶向直肠癌肿瘤细胞。 抗体与西妥昔单抗联合用药的抑瘤效果也优于单用抗体或西妥昔单抗。
Impact of polyunsaturated and saturated fat overfeeding on the DNA-methylation pattern in human adipose tissue: a randomized controlled trial
DNA methylation epigenetics EWAS Illumina 450k methylation array LIPOGAIN cohort obesity overfeeding polyunsaturated fat prediction saturated fat
2018/11/13
Background: Dietary fat composition can affect ectopic lipid accumulation and, thereby, insulin resistance. Diets that are high in saturated fatty acids (SFAs) or polyunsaturated fatty acids (PUFAs) h...
Alterations in human milk leptin and insulin are associated with early changes in the infant intestinal microbiome
milk leptin insulin the infant intestinal microbiome
2018/11/12
We read with great interest the study by Lemas et al. (1) that reported early changes in the gut microbiota composition and functions of exclusively breastfed infants born from obese mothers compared ...
Electrostatic Fields Near the Active Site of Human Aldose Reductase:1.New Inhibitors and Vibrational Stark Effect Measurements
apoptosis ATM cisplatin IKK p73 ubiquitination
2016/5/25
Vibrational Stark effect spectroscopy was used to measure electrostatic fields in the hydrophobic region of the active site of human aldose reductase (hALR2). A new hALR2 inhibitor was designed and sy...
Spectroscopic Study of Ser92 Mutants of Human Myoglobin:Hydrogen Bonding Effect of Ser92 to Proximal His93 on Structure and Property of Myoglobin
Carbon Monoxide Cyanides Escherichia coli Ferric Compounds Ferrous Compounds Histidine Humans Hydrogen Bonding Magnetic Resonance Spectroscopy Mutagenesis Myoglobin Myoglobin Oxygen Polymerase Chain Reaction Recombinant Fusion Proteins Serine Serine Spectrophotometr Spectrum Analysis, Raman Structure-Activity Relationship
2016/5/23
Neutron diffraction studies have demonstrated that the hydroxyl group oxygen of Ser92(F7) is hydrogen bonded to the proximal His93(48) N epsilon H proton in myoglobin (Mb) [Cheng, X., & Shoenborn, B. ...
Ultrafast Measurements of Geminate Recombination of NO with Site-specific Mutants of Human Myoglobin
human myoglobin mutagenesis kinetics structure-function relationships picosecond timescale
2016/5/23
Flash photolysis studies of NO recombination to heme proteins offer a direct probe of protein structural changes on the tens of picoseconds timescale where they can be compared with molecular dynamics...
Dynamics of Protein Relaxation in Site-Specific Mutants of Human Myoglobin
Humans Cysteine Heme Alanine Myoglobin Recombinant Proteins Spectrophotometry Mutagenesis,Site-Directed Amino Acid Sequence Protein Conformation
2016/5/23
We have recently reported spectroscopic evidence for structural relaxation of myoglobin (Mb) following photodissociation of MbCO [Lambright, D. G., Balasubramanian, S., & Boxer, S. G. (1991) Chem. Phy...
Perturbations of the Distal Heme Pocket in Human Myoglobin Mutants Probed by Infrared Spectroscopy of Bound CO:Correlation with Ligand Binding Kinetics
Distal Heme Pocket Human Myoglobin Mutants Probed Infrared Spectroscopy Bound CO:Correlation Ligand Binding Kinetics
2016/5/23
The infrared spectra of CO bound to human myoglobin and myoglobin mutants at positions His-64, Val-68, Asp-60, and Lys-45 on the distal side have been measured between 100 and 300 K. Large differences...
CO Recombination to Human Myoglobin Mutants in Glycerol-Water Solutions
CO Recombination Human Myoglobin Mutants Glycerol-Water Solutions
2016/5/23
The kinetics of CO recombination to site-specific mutants of human myoglobin have been studied by flash photolysis in the temperature range 250-320 K on the nanosecond to second time scale in 75% glyc...
X-ray Crystal Structure of a Mutant Recombinant Human Myoglobin at 2.8Å Resolution
Humans Myoglobin Recombinant Proteins X-Ray Diffraction Protein Conformation Mutation Molecular Structure
2016/5/23
We have grown crystals in trigonal space group P 3 2 21 of a mutant human myoglobin, aquomet form, in which lysine at position 45 has been replaced by arginine and cysteine at position 110 has been re...
Electrostatic Interactions in Wild Type and Mutant Recombinant Human Myoglobins
SUBSTANCE-P GABA PROLACTIN ANTERIOR PITUITARY HYPOTHALAMIC FRAGMENTS ANTI-SUBSTANCE-P SERUM
2016/5/20
Residue Val68 in human myoglobin has been replaced by Asn, Asp, and Glu with site-directed mutagenesis. Purified proteins were characterized by isoelectric focusing and by absorption, CD, and NMR spec...
Ligand and Proton Exchange Dynamics in Recombinant Human Myoglobin Mutants
Mb myoglobin n.m.r. nuclear magnetic resonance fwhm full width at half maximum TSP sodium 3-trimethyl silyl propionate DSS 4,4-dimethyl-4-sila pentane-1-sulfonate
2016/5/20
Site-specific mutants of human myoglobin have been prepared in which lysine 45 is replaced by arginine (K45R) and aspartate 60 by glutamate (D60E), in order to examine the influence of these residues ...
Identification of Tobacco-Related Compounds in Tobacco Products and Human Hair
Dissolvable Tobacco Solid Phase Microextraction Tobacco Biomarkers
2015/5/21
Analyses of tobacco products and their usage are well-researched and have implications in analytical chemistry, forensic science, toxicology, and medicine. As such, analytical methods must be develope...
Structure, Function, and Pharmacological Chaperones for Human α-N-Acetylgalactosaminidase
Pure sciences Biological sciences Galactosidase Acetylgalactosaminidase Lysosomal storage disease Pharmacological chaperones Structural biology X-ray crystallography
2014/12/10
Human lysosomal α-N-acetylgalactosaminidase (α-NAGAL) is responsible for the break down of glycolipids and glycopeptides that contain a terminal α-linked N-acetylgalactosamine residues. Deficiency of ...
Structural And Biochemical Studies Of The Human Lysosomal Enzymes: N-Acetylgalactosamine-6-Sulfatase, N-Sulfoglucosamine Sulfohydrolase And Beta-Galactosidase
Pure sciences Biological sciences Cysteine modification Enzyme replacement therapy Lysosomal storage disease Pharmacological chaperone therapy Sulfatase structure X-ray crystallography
2014/12/10
Lysosomal storage diseases are disorders caused by deficiencies of enzymes responsible for the degradation of substances present in lysosomes. The loss of activity of a lysosomal enzyme leads to the a...