10 results on '"Zhuoying Yang"'
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2. Self‐assembly Behavior of Metal Halide Perovskite Nanocrystals
- Author
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Zhuoying Yang, Shaomin Peng, Fan Lin, Pengfei Wang, Guichuan Xing, and Lin Yu
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General Chemistry - Published
- 2022
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3. Preparation of Hydrated TiO2 Particles by Hydrothermal Hydrolysis of Mg/Al-Bearing TiOSO4 Solution
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Shuyu Lin, Fan Yang, Zhuoying Yang, Jing Wang, and Lan Xiang
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General Chemical Engineering ,General Materials Science ,hydrated TiO2 ,TiOSO4 ,hydrothermal hydrolysis ,MgSO4 and Al2(SO4)3 - Abstract
As the byproduct in the smelting process of vanadium titano-magnetite, titanium-bearing blast furnace slag (TBFS) can be converted to a titanyl sulfate (TiOSO4) solution containing MgSO4 and Al2(SO4)3 impurities via dissociation by concentrated H2SO4 (80–95%) at 80–200 °C, followed by leaching with H2O at 60–85 °C. In this study, hydrated TiO2 was prepared by hydrothermal hydrolysis of a Mg/Al-bearing TiOSO4 solution at 120 °C and the hydrolysis law was investigated. The experimental results indicate that MgSO4 and Al2(SO4)3 accelerated the hydrolysis and significantly affected the particle size (increasing the primary agglomerate size from 40 to 140 nm) and dispersion (reducing the aggregate size from 12.4 to 1.5 μm) of hydrated TiO2. A thermodynamic equilibrium calculation showed TiOSO4 existed as TiO2+ and SO42− in the solution, and MgSO4 and Al2(SO4)3 led to little change of [TiO2+], but an obvious decrease of [H+], which favored the hydrolysis process. At the same time, the coordination–dissociation mechanism of SO42− and Al(SO4)2− facilitated the lap bonding of Ti-O-Ti, promoting the growth of hydrated TiO2 synergistically.
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- 2023
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4. The KATP channel opener, nicorandil, ameliorates brain damage by modulating synaptogenesis after ischemic stroke
- Author
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Zhuoying Yang, Yuanzheng Zhao, Heping Yuan, Ruonan Sun, and Yuan-Hong He
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Physiology ,Vasodilator Agents ,Synaptogenesis ,Artificial Gene Amplification and Extension ,Pharmacology ,Vascular Medicine ,Polymerase Chain Reaction ,Hippocampus ,Rats, Sprague-Dawley ,Medical Conditions ,KATP Channels ,Immunofluorescence Staining ,Animal Cells ,Blood Flow ,Medicine and Health Sciences ,Brain Damage ,Nicorandil ,Staining ,Neurons ,Multidisciplinary ,biology ,Cerebral infarction ,Brain ,Body Fluids ,Stroke ,Neuroprotective Agents ,Blood ,Neurology ,Cerebral blood flow ,Infarction ,Cerebrovascular Circulation ,cardiovascular system ,Medicine ,Anatomy ,Cellular Types ,medicine.symptom ,Research Article ,medicine.drug ,Cerebrovascular Diseases ,Science ,Brain damage ,Research and Analysis Methods ,Neuroprotection ,Cerebral edema ,Signs and Symptoms ,medicine ,Animals ,Molecular Biology Techniques ,Molecular Biology ,Ischemic Stroke ,business.industry ,Biology and Life Sciences ,Reverse Transcriptase-Polymerase Chain Reaction ,Cell Biology ,medicine.disease ,Rats ,Specimen Preparation and Treatment ,Cellular Neuroscience ,Synapses ,biology.protein ,Clinical Medicine ,NeuN ,business ,Neuroscience - Abstract
With population growth and aging, more and more patients with cerebral infarction have varying degrees of disability. ATP-sensitive potassium (KATP) channels regulate many cellular functions by coupling metabolic status with cell membrane electrical activity. Nicorandil (N-(2-hydroxyethyl)-nicotinamide nitrate) is the first KATP channel opener approved for clinical use. It has been reported that it might exert protective effects on the cerebral infarction by increasing cerebral blood flow and reducing inflammation. However, only a few studies explored its role in synaptogenesis. We made the rat model of middle cerebral artery occlusion (MCAO). Nicorandil was administered to rats via oral administration immediately after the surgery at a dose of 7.5 mg/kg and then daily for the next days. Infarct volume, cerebral edema, neurological deficits, cognitive impairment, and the level of Synaptophysin (SYP)、Growth associated protein-43 (GAP43) and neuronal nuclear antigen (NeuN) levels were measured to evaluate the effect of nicorandil. Our data showed that nicorandil treatment could decrease brain damage, improve learning and memory, and increase SYP、GAP43 and NeuN level. Taken together, we propose that nicorandil, as an opener of the KATP channel, provides a neuroprotective role in MCAO by promoting synaptic connections.
- Published
- 2021
5. Dock5 activation facilitates diabetic wound healing
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Zhuo-Xian Meng and Zhuoying Yang
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Editorial ,Text mining ,Physiology ,business.industry ,Diabetic wound healing ,MEDLINE ,QP1-981 ,Medicine ,QD415-436 ,Bioinformatics ,business ,Biochemistry - Published
- 2021
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6. Estrogen Modulation of Apolipoprotein(a) Expression
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Richard M. Lawn, Dario Boffelli, Zhuoying Yang, and Deborah A. Zajchowski
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Hormone response element ,medicine.drug_class ,Cell Biology ,Biology ,Biochemistry ,Lipoprotein particle ,Molecular biology ,Transactivation ,Estrogen ,Chromosomal region ,medicine ,Molecular Biology ,Estrogen receptor alpha ,Transcription factor ,hormones, hormone substitutes, and hormone antagonists ,Estrogen receptor beta - Abstract
Elevated plasma levels of the lipoprotein particle Lp(a) are a major risk factor for cardiovascular disease. Lp(a) plasma levels are determined by the level of expression of its characteristic protein component, apo(a). Apo(a) expression is modulated by several hormones, of which estrogens are the best known. The chromosomal region responsible for estrogen response was identified within an apo(a) enhancer located at approximately 26 kilobases from the apo(a) promoter. Although the estrogen-responsive unit contains a potential estrogen response element, binding of estrogen receptor-alpha to DNA was not necessary. The receptor, activated by bound estradiol, interacts through its transactivation domains with a transcription factor necessary for the function of the enhancer, preventing its binding to DNA.
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- 1999
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7. Human GATA-3 trans-activation, DNA-binding, and nuclear localization activities are organized into distinct structural domains
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Hozumi Motohashi, Lin Gu, Paul-Henri Romeo, James Douglas Engel, Dominique Bories, Zhuoying Yang, and Masayuki Yamamoto
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Transcription, Genetic ,Recombinant Fusion Proteins ,Molecular Sequence Data ,GATA3 Transcription Factor ,Biology ,DNA-binding protein ,Cell Line ,Structure-Activity Relationship ,Humans ,Molecular Biology ,Transcription factor ,Gene ,DNA Primers ,Sequence Deletion ,Zinc finger transcription factor ,Zinc finger ,chemistry.chemical_classification ,Sp1 transcription factor ,Base Sequence ,Antibodies, Monoclonal ,Nuclear Proteins ,Zinc Fingers ,Cell Biology ,Cell Compartmentation ,Amino acid ,DNA-Binding Proteins ,RING finger domain ,Biochemistry ,chemistry ,embryonic structures ,Trans-Activators ,Research Article - Abstract
GATA-3 is a zinc finger transcription factor which is expressed in a highly restricted and strongly conserved tissue distribution pattern in vertebrate organisms, specifically, in a subset of hematopoietic cells, in cells within the central and peripheral nervous systems, in the kidney, and in placental trophoblasts. Tissue-specific cellular genes regulated by GATA-3 have been identified in T lymphocytes and the placenta, while GATA-3-regulated genes in the nervous system and kidney have not yet been defined. We prepared monoclonal antibodies with which we could dissect the biochemical and functional properties of human GATA-3. The results of these experiments show some anticipated phenotypes, for example, the definition of discrete domains required for specific DNA-binding site recognition (amino acids 303 to 348) and trans activation (amino acids 30 to 74). The signaling sequence for nuclear localization of human GATA-3 is a property conferred by sequences within and surrounding the amino finger (amino acids 249 to 311) of the protein, thereby assigning a function to this domain and thus explaining the curious observation that this zinc finger is dispensable for DNA binding by the GATA family of transcription factors.
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- 1994
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8. Structure and regulation of the chicken erythroid δ-aminolevulinate synthase gene
- Author
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Nancy C. Andrews, James Douglas Engel, Hajime Ishihara, Zhuoying Yang, Kim Chew Lim, Robert D. Riddle, and Masayuki Yamamoto
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Untranslated region ,Erythrocytes ,Transcription, Genetic ,Molecular Sequence Data ,Restriction Mapping ,Heme ,Regulatory Sequences, Nucleic Acid ,Biology ,Gene Expression Regulation, Enzymologic ,Exon ,Transcription (biology) ,Sequence Homology, Nucleic Acid ,Genetics ,Transcriptional regulation ,Animals ,Humans ,Promoter Regions, Genetic ,Gene ,Base Sequence ,Intron ,RNA ,DNA ,Exons ,Molecular biology ,Regulatory sequence ,Chickens ,Cell Division ,5-Aminolevulinate Synthetase - Abstract
Erythroid cells regulate heme biosynthesis in a manner that is distinct from all other cell types. While heme negatively regulates the synthesis of the housekeeping delta-aminolevulinate synthase (ALAS-N) in all non-erythroid cells, the expression of an erythroid-specific isozyme (ALAS-E) is developmentally regulated in red blood cells. As a first step towards understanding the molecular basis for the transcriptional regulation of ALAS-E during erythropoiesis, we cloned and characterized the chicken ALAS-E locus. This gene spans 18 kbp and is composed of eleven exons. The intron/exon structure of erythroid ALAS was found to be conserved among several vertebrate species. Direct RNA sequencing identified a 5' untranslated region that is derived from two continuous exons and is predicted to form a very stable stem-loop structure that bears resemblance to the ferritin iron-responsive element. Tissue-specific expression of the ALAS-E gene was analyzed by transient transfection assays in hematopoietic cells of both erythroid and non-erythroid origins. These experiments identified distal (-784 to -505 bp) and proximal (-155 to +21 bp) promoter elements which are required for high level, erythroid-specific transcription.
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- 1994
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9. Apolipoprotein(a) gene enhancer resides within a LINE element
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Dario Boffelli, Karen Schwartz, Zhuoying Yang, Nataya W. Boonmark, and Richard M. Lawn
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Apolipoprotein B ,Transcription, Genetic ,Molecular Sequence Data ,Retrotransposon ,Enhancer RNAs ,Biology ,Apoprotein(a) ,Biochemistry ,Transcription (biology) ,Tumor Cells, Cultured ,Humans ,Nuclear protein ,Enhancer ,Molecular Biology ,Gene ,Sequence Deletion ,Base Sequence ,Cell Biology ,DNA ,Molecular biology ,Apolipoproteins ,Enhancer Elements, Genetic ,biology.protein ,Mutagenesis, Site-Directed ,Lipoprotein ,Lipoprotein(a) - Abstract
Apolipoprotein(a), (apo(a)), is the distinguishing protein portion of the lipoprotein(a) particle, elevated plasma levels of which are a major risk factor for cardiovascular disease. A search for enhancer elements that control the transcription of the apo(a) gene led to the identification of an upstream element that contains target binding sites for members of the Ets and Sp1 nuclear protein families. The enhancer element functions in either orientation to confer a greater than 10-fold increase in the activity of the apo(a) minimal promoter in cultured hepatocyte cells. Unexpectedly, the enhancer element is located within a LINE retrotransposon element, suggesting that LINE elements may function as mobile regulatory elements to control the expression of nearby genes.
- Published
- 1998
10. The beta-globin stage selector element factor is erythroid-specific promoter/enhancer binding protein NF-E4
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James Douglas Engel, J. L. Gallarda, Zhuoying Yang, and K. P. Foley
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Erythrocytes ,Transcription, Genetic ,Blotting, Western ,Molecular Sequence Data ,Radioimmunoassay ,Chick Embryo ,Biology ,Transfection ,DNA-binding protein ,Transcription (biology) ,Genetics ,Animals ,Enhancer trap ,Globin ,Promoter Regions, Genetic ,Enhancer ,Gene ,Erythroid Precursor Cells ,Base Sequence ,Binding protein ,Globins ,Enhancer Elements, Genetic ,Biochemistry ,Chickens ,Transcription Factors ,Developmental Biology - Abstract
The analysis of transcriptional regulatory proteins is often hampered because such factors are present in cells in only sparing abundance. Although direct biochemical purification has been successfully applied to the analysis of many of these factors, such methods are labor intensive and expensive. We have developed an alternative strategy to identify and characterize such trans-acting factors and have used it to analyze the proteins that interact with the chicken adult beta-globin gene enhancer and promoter. The methodology involves (1) a sensitive 'reverse' radioimmunoassay used for the identification of antibodies to sequence-specific DNA-binding proteins, and (2) a monoclonal antibody-based DNase I footprint selection technique, which unambiguously identifies proteins responsible for particular footprints. Because this methodology relies on the isolation of antibodies to sequence-specific DNA-binding proteins, it should be of general utility in studying any trans-acting regulatory factor for which a specific DNA-binding sequence can be identified. In the present analysis, we report the identification of a 65-kD protein that is present only in mature definitive (adult) chicken erythroid cells. We show that this protein (termed NF-E4) binds to closely related sequences present in both the beta-globin promoter and enhancer. Biochemical analysis of extracts prepared from both nonerythroid and a variety of erythroid cell types suggests that NF-E4 is the trans-acting factor that confers definitive erythrocyte stage-specific transcriptional activation to the adult beta-globin gene.
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- 1989
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