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  1. AU="Tran, Thuy Van"
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  1. Article ; Online: The relationship between population growth and precipitation change in some regions across Vietnam: implications for urbanization effect.

    Pham, Viet Anh T / Tran, Toan Kim / Nguyen, Khai Manh / Tran, Thuy Van / Vu, Ly Huong / Pham, Ha T T

    Environmental science and pollution research international

    2024  Volume 31, Issue 10, Page(s) 15007–15025

    Abstract: According to a review of numerous publications and scientific reports, the effects of urbanization on urban climate are of greatest concern. This study aims to evaluate the impact of urbanization focusing on population growth on precipitation trends in ... ...

    Abstract According to a review of numerous publications and scientific reports, the effects of urbanization on urban climate are of greatest concern. This study aims to evaluate the impact of urbanization focusing on population growth on precipitation trends in 11 provinces across Vietnam during the period 2008-2018 by identifying the relationship between population growth and precipitation change. Regression analysis is used to determine the trends of precipitation and population growth. Precipitation maps and graphs show the overall precipitation trends, changes, and patterns in past decades. Overall, population growth tends to correlate with precipitation change trends. Furthermore, the type of region groups (countryside region, small city, or medium city) also plays a crucial role in determining the magnitude of the change in precipitation trends for each region. This further lends credibility to the notion that urbanization contributes to changes in precipitation trends.
    MeSH term(s) Humans ; Urbanization ; Population Growth ; Urban Population ; Demography ; Vietnam ; Geography ; Developing Countries
    Language English
    Publishing date 2024-01-29
    Publishing country Germany
    Document type Review ; Journal Article
    ZDB-ID 1178791-0
    ISSN 1614-7499 ; 0944-1344
    ISSN (online) 1614-7499
    ISSN 0944-1344
    DOI 10.1007/s11356-024-32039-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Dexamethasone effects on group B streptococcal infection in newborn rats.

    Tran, Thuy-Van P / Weisman, Leonard E

    The Pediatric infectious disease journal

    2004  Volume 23, Issue 1, Page(s) 47–52

    Abstract: Background: We previously published that human neutrophil-mediated bacterial killing of group B Streptococcus (GBS) in vitro was dependent on the timing and concentration of dexamethasone exposure.: Hypothesis: Dexamethasone treatment would affect ... ...

    Abstract Background: We previously published that human neutrophil-mediated bacterial killing of group B Streptococcus (GBS) in vitro was dependent on the timing and concentration of dexamethasone exposure.
    Hypothesis: Dexamethasone treatment would affect neutrophil mediated killing of GBS in an animal model.
    Methods: Wistar rat pups were randomly allocated to receive placebo or dexamethasone before, early or late after GBS infection. Suckling rats were infected with 104 or 105 colony-forming units of GBS or nothing. Pups were followed for survival, quantitative bacteremia, growth and neutrophil-mediated bacterial killing. Neutrophils for bacterial killing were obtained via cardiac puncture before infection. Statistics included chi square for survival, Mann-Whitney U test for bacteremia, analysis of variance for growth and paired Student's t test for bacterial killing analyses.
    Results: Dexamethasone treatment before invasive GBS infection decreases quantitative bacteremia, improves survival and improves neonatal neutrophil-mediated bacterial killing in suckling rats, whereas dexamethasone treatment after infection increases bacteremia and decreases survival. Regardless of timing of dexamethasone treatment, before or after invasive GBS infection, growth was significantly impaired in all suckling rats receiving dexamethasone compared with controls.
    Conclusion: Treatment with dexamethasone before invasive GBS infection improves survival and decreases bacteremia in suckling rats; this appears in part to be mediated by improved neonatal neutrophil-mediated bacterial killing. We speculate that this improvement in outcome may be a result of improved number or function of neutrophil cell surface receptors.
    MeSH term(s) Animals ; Animals, Newborn ; Bacteremia/drug therapy ; Dexamethasone/pharmacology ; Disease Models, Animal ; Dose-Response Relationship, Drug ; Drug Administration Schedule ; Female ; Male ; Probability ; Random Allocation ; Rats ; Reference Values ; Sensitivity and Specificity ; Streptococcal Infections/drug therapy ; Streptococcal Infections/mortality ; Streptococcus agalactiae/drug effects ; Survival Rate
    Chemical Substances Dexamethasone (7S5I7G3JQL)
    Language English
    Publishing date 2004-01
    Publishing country United States
    Document type Comparative Study ; Journal Article
    ZDB-ID 392481-6
    ISSN 1532-0987 ; 0891-3668
    ISSN (online) 1532-0987
    ISSN 0891-3668
    DOI 10.1097/01.inf.0000105107.76541.ee
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: The stalk domain and the glycosylation status of the activating natural killer cell receptor NKp30 are important for ligand binding.

    Hartmann, Jessica / Tran, Thuy-Van / Kaudeer, Janina / Oberle, Karin / Herrmann, Julia / Quagliano, Isabell / Abel, Tobias / Cohnen, André / Gatterdam, Volker / Jacobs, Andrea / Wollscheid, Bernd / Tampé, Robert / Watzl, Carsten / Diefenbach, Andreas / Koch, Joachim

    The Journal of biological chemistry

    2012  Volume 287, Issue 37, Page(s) 31527–31539

    Abstract: The natural cytotoxicity receptors are a unique set of activating proteins expressed mainly on the surface of natural killer (NK) cells. The human natural cytotoxicity receptor family comprises the three type I membrane proteins NKp30, NKp44, and NKp46. ... ...

    Abstract The natural cytotoxicity receptors are a unique set of activating proteins expressed mainly on the surface of natural killer (NK) cells. The human natural cytotoxicity receptor family comprises the three type I membrane proteins NKp30, NKp44, and NKp46. Especially NKp30 is critical for the cytotoxicity of NK cells against different targets including tumor, virus-infected, and immature dendritic cells. Although the crystal structure of NKp30 was recently solved (Li, Y., Wang, Q., and Mariuzza, R. A. (2011) J. Exp. Med. 208, 703-714; Joyce, M. G., Tran, P., Zhuravleva, M. A., Jaw, J., Colonna, M., and Sun, P. D. (2011) Proc. Natl. Acad. Sci. U.S.A. 108, 6223-6228), a key question, how NKp30 recognizes several non-related ligands, remains unclear. Therefore, we investigated the parameters that impact ligand recognition of NKp30. Based on various NKp30-hIgG1-Fc fusion proteins, which were optimized for minimal background binding to cellular Fcγ receptors, we identified the flexible stalk region of NKp30 as an important but so far neglected module for ligand recognition and related signaling of the corresponding full-length receptor proteins. Moreover, we found that the ectodomain of NKp30 is N-linked glycosylated at three different sites. Mutational analyses revealed differential binding affinities and signaling capacities of mono-, di-, or triglycosylated NKp30, suggesting that the degree of glycosylation could provide a switch to modulate the ligand binding properties of NKp30 and NK cell cytotoxicity.
    MeSH term(s) Animals ; CHO Cells ; COS Cells ; Chlorocebus aethiops ; Cricetinae ; Cricetulus ; Glycosylation ; HEK293 Cells ; Humans ; Immunity, Cellular/physiology ; K562 Cells ; Killer Cells, Natural/cytology ; Killer Cells, Natural/immunology ; Killer Cells, Natural/pathology ; Mutation ; Natural Cytotoxicity Triggering Receptor 3/genetics ; Natural Cytotoxicity Triggering Receptor 3/immunology ; Natural Cytotoxicity Triggering Receptor 3/metabolism ; Oligosaccharides/genetics ; Oligosaccharides/metabolism ; Protein Structure, Tertiary/physiology ; Receptors, IgG/genetics ; Receptors, IgG/metabolism
    Chemical Substances NCR3 protein, human ; Natural Cytotoxicity Triggering Receptor 3 ; Oligosaccharides ; Receptors, IgG
    Language English
    Publishing date 2012-07-17
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M111.304238
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Catalysis leads to posttranslational inactivation of the type 1 deiodinase and alters its conformation.

    Zhu, Bo / Shrivastava, Ashutosh / Luongo, Cristina / Chen, Ting / Harney, John W / Marsili, Alessandro / Tran, Thuy-Van / Bhadouria, Anulika / Mopala, Radhika / Steen, Amanda I / Larsen, P Reed / Zavacki, Ann Marie

    The Journal of endocrinology

    2012  Volume 214, Issue 1, Page(s) 87–94

    Abstract: Previously, it was shown that the type 1 deiodinase (D1) is subject to substrate-dependent inactivation that is blocked by pretreatment with the inhibitor of D1 catalysis, propylthiouracil (PTU). Using HepG2 cells with endogenous D1 activity, we found ... ...

    Abstract Previously, it was shown that the type 1 deiodinase (D1) is subject to substrate-dependent inactivation that is blocked by pretreatment with the inhibitor of D1 catalysis, propylthiouracil (PTU). Using HepG2 cells with endogenous D1 activity, we found that while considerable D1-mediated catalysis of reverse tri-iodothyronine (rT(3)) is observed in intact cells, there was a significant loss of D1 activity in sonicates assayed from the same cells in parallel. This rT(3)-mediated loss of D1 activity occurs despite no change in D1 mRNA levels and is blocked by PTU treatment, suggesting a requirement for catalysis. Endogenous D1 activity in sonicates was inactivated in a dose-dependent manner in HepG2 cells, with a ∼50% decrease after 10 nM rT(3) treatment. Inactivation of D1 was rapid, occurring after only half an hour of rT(3) treatment. D1 expressed in HEK293 cells was inactivated by rT(3) in a similar manner. (75)Se labeling of the D1 selenoprotein indicated that after 4 h rT(3)-mediated inactivation of D1 occurs without a corresponding decrease in D1 protein levels, though rT(3) treatment causes a loss of D1 protein after 8-24 h. Bioluminescence resonance energy transfer studies indicate that rT(3) exposure increases energy transfer between the D1 homodimer subunits, and this was lost when the active site of D1 was mutated to alanine, suggesting that a post-catalytic structural change in the D1 homodimer could cause enzyme inactivation. Thus, both D1 and type 2 deiodinase are subject to catalysis-induced loss of activity although their inactivation occurs via very different mechanisms.
    MeSH term(s) Biocatalysis/drug effects ; Dose-Response Relationship, Drug ; Enzyme Activation/drug effects ; Fluorescence Resonance Energy Transfer ; HEK293 Cells ; Hep G2 Cells ; Humans ; Iodide Peroxidase/chemistry ; Iodide Peroxidase/genetics ; Iodide Peroxidase/metabolism ; Luciferases/genetics ; Luciferases/metabolism ; Luminescent Proteins/genetics ; Luminescent Proteins/metabolism ; Mutation ; Propylthiouracil/pharmacology ; Protein Conformation ; Protein Multimerization ; Protein Processing, Post-Translational/drug effects ; Reverse Transcriptase Polymerase Chain Reaction ; Sonication ; Substrate Specificity ; Triiodothyronine/metabolism ; Triiodothyronine/pharmacology
    Chemical Substances Luminescent Proteins ; Triiodothyronine (06LU7C9H1V) ; Propylthiouracil (721M9407IY) ; iodothyronine deiodinase type I (EC 1.11.1.-) ; Iodide Peroxidase (EC 1.11.1.8) ; Luciferases (EC 1.13.12.-)
    Language English
    Publishing date 2012-04-27
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 3028-4
    ISSN 1479-6805 ; 0022-0795
    ISSN (online) 1479-6805
    ISSN 0022-0795
    DOI 10.1530/JOE-11-0459
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Uh III Zs.133: Show issues Location:
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