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  1. Article: [Glucose-6 phosphatase catalytic subunit inhibits the proliferation of liver cancer cells by inducing cell cycle arrest].

    Lin, X / Pan, X M / Peng, Z K / Wang, K / Tang, N

    Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology

    2022  Volume 30, Issue 2, Page(s) 213–219

    Abstract: Objective: ...

    Abstract Objective:
    MeSH term(s) Catalytic Domain ; Cell Cycle Checkpoints ; Cell Line, Tumor ; Cell Proliferation ; Gene Expression Regulation, Neoplastic ; Glucose-6-Phosphatase/metabolism ; Humans ; Liver Neoplasms/genetics
    Chemical Substances Glucose-6-Phosphatase (EC 3.1.3.9)
    Language Chinese
    Publishing date 2022-03-28
    Publishing country China
    Document type Journal Article
    ISSN 1007-3418
    ISSN 1007-3418
    DOI 10.3760/cma.j.cn501113-20210204-00067
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: [Immunologic changes during hyposensitization with the dust mite Dermatophagoides farinae extract in allergic asthma].

    Peng, Z K

    Zhonghua jie he he hu xi xi ji bing za zhi = Chinese journal of tuberculosis and respiratory diseases

    1985  Volume 8, Issue 4, Page(s) 207–10, 254–5

    MeSH term(s) Asthma/immunology ; Asthma/therapy ; Desensitization, Immunologic ; Humans ; Immunoglobulin E/analysis ; Immunoglobulin G/analysis ; Mites/immunology
    Chemical Substances Immunoglobulin G ; Immunoglobulin E (37341-29-0)
    Language Chinese
    Publishing date 1985-08
    Publishing country China
    Document type English Abstract ; Journal Article
    ZDB-ID 604670-8
    ISSN 0253-2689
    ISSN 0253-2689
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.B 2465: Show issues Location:
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  3. Article ; Online: Very-high-frequency oscillations in the main peak of a magnetar giant flare.

    Castro-Tirado, A J / Østgaard, N / Göǧüş, E / Sánchez-Gil, C / Pascual-Granado, J / Reglero, V / Mezentsev, A / Gabler, M / Marisaldi, M / Neubert, T / Budtz-Jørgensen, C / Lindanger, A / Sarria, D / Kuvvetli, I / Cerdá-Durán, P / Navarro-González, J / Font, J A / Zhang, B-B / Lund, N /
    Oxborrow, C A / Brandt, S / Caballero-García, M D / Carrasco-García, I M / Castellón, A / Castro Tirado, M A / Christiansen, F / Eyles, C J / Fernández-García, E / Genov, G / Guziy, S / Hu, Y-D / Nicuesa Guelbenzu, A / Pandey, S B / Peng, Z-K / Pérez Del Pulgar, C / Reina Terol, A J / Rodríguez, E / Sánchez-Ramírez, R / Sun, T / Ullaland, K / Yang, S

    Nature

    2021  Volume 600, Issue 7890, Page(s) 621–624

    Abstract: Magnetars are strongly magnetized, isolated neutron ... ...

    Abstract Magnetars are strongly magnetized, isolated neutron stars
    MeSH term(s) Atmosphere ; Stars, Celestial
    Language English
    Publishing date 2021-12-22
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-021-04101-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Production and characterization of monoclonal antibodies to two new mosquito Aedes aegypti salivary proteins

    Peng, Z.K / Yang, J / Wang, H.S / Simons, F.E.R

    Insect biochemistry and molecular biology. Oct 1999. v. 29 (10)

    1999  

    Abstract: Mosquito salivary proteins, which are fundamental to the process of blood feeding, also facilitate disease transmission and cause allergic reactions. The identification and characterisation of these proteins have been hampered by the difficulty of ... ...

    Abstract Mosquito salivary proteins, which are fundamental to the process of blood feeding, also facilitate disease transmission and cause allergic reactions. The identification and characterisation of these proteins have been hampered by the difficulty of obtaining them in purified form. In this report, we describe the production of mouse monoclonal antibodies (mAbs) against mosquito salivary proteins. BALB/c mice were immunised with Aedes aegypti saliva proteins. Hybridomas were produced by fusion of spleen cells with a mouse myeloma cell line. Positive clones were selected using a saliva-capture ELISA and further identified using immunoblotting. Three mAbs reacted with a 44 kDa protein (Aed a X(1)) in the saliva-immunoblotting, and did not react with 2 recombinant salivary proteins, rAed a 1 (apyrase) and rAed a 2 (D7), in both immunoblotting and ELISA. Two other mAbs reacted with a 37 kDa protein in saliva-immunoblotting, but failed to react with the 37 kDa rAed a 2 in either immunoblotting or ELISA, suggesting that there is a second 37 kDa protein (Aed a X(2)) which is recognised by the two mAbs. The 44 kDa and 37 kDa proteins have not been previously identified. These mAbs provide a means to purify proteins, to isolate new genes from the salivary gland cDNA library, and to standardise mosquito extracts, facilitating studies of disease transmission by mosquitoes and of mosquito allergy.
    Keywords Aedes aegypti ; saliva ; animal proteins ; monoclonal antibodies ; antibody formation ; hybridomas ; immunoblotting ; enzyme-linked immunosorbent assay ; Western blotting
    Language English
    Dates of publication 1999-10
    Size p. 909-914.
    Document type Article
    ZDB-ID 1483248-3
    ISSN 1879-0240 ; 0965-1748
    ISSN (online) 1879-0240
    ISSN 0965-1748
    Database NAL-Catalogue (AGRICOLA)

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  5. Article: Differential binding properties of protein A and protein G for dog immunoglobulins.

    Peng, Z K / Simons, F E / Becker, A B

    Journal of immunological methods

    1991  Volume 145, Issue 1-2, Page(s) 255–258

    Abstract: We studied the binding of dog immunoglobulins G, A, M and E to protein A and protein G. Passive cutaneous anaphylaxis (PCA) testing was used for the measurement of dog IgE and enzyme-linked immunosorbent assays (ELISA) were used for the measurements of ... ...

    Abstract We studied the binding of dog immunoglobulins G, A, M and E to protein A and protein G. Passive cutaneous anaphylaxis (PCA) testing was used for the measurement of dog IgE and enzyme-linked immunosorbent assays (ELISA) were used for the measurements of dog IgG, IgA and IgM. Protein A from lyophilized cells of Staphylococcus aureus bound 97% of IgE, 98% of IgG, 81% of IgA, and 97% of IgM. Protein A-Sepharose CL-4B bound 87% of IgE, 100% of IgG and IgA, and 98% of IgM. In a stepwise elution with varying pH, a small amount of IgE was eluted at pH 5 and pH 6 and all the remaining Igs were eluted at pH 3 from the protein A column. In contrast to protein A, dog IgE was not bound to Protein G-Sepharose, while 100% of IgG, 95% of IgA, and 44% of IgM were bound to Protein G-Sepharose.
    MeSH term(s) Animals ; Bacterial Proteins/immunology ; Chromatography, Affinity ; Dogs/immunology ; Immunoglobulin A/metabolism ; Immunoglobulin E/metabolism ; Immunoglobulin G/metabolism ; Immunoglobulin M/metabolism ; Immunoglobulins/metabolism ; Protein Binding ; Staphylococcal Protein A/metabolism
    Chemical Substances Bacterial Proteins ; IgG Fc-binding protein, Streptococcus ; Immunoglobulin A ; Immunoglobulin G ; Immunoglobulin M ; Immunoglobulins ; Staphylococcal Protein A ; Immunoglobulin E (37341-29-0)
    Language English
    Publishing date 1991-12-15
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120142-6
    ISSN 1872-7905 ; 0022-1759
    ISSN (online) 1872-7905
    ISSN 0022-1759
    DOI 10.1016/0022-1759(91)90335-d
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 795: Show issues Location:
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  6. Article: Quantitative IgE- and IgG-subclass responses during and after long-term ragweed immunotherapy.

    Peng, Z K / Naclerio, R M / Norman, P S / Adkinson, N F

    The Journal of allergy and clinical immunology

    1992  Volume 89, Issue 2, Page(s) 519–529

    Abstract: We studied the quantitative responses of short ragweed (RW)-pollen-specific serum antibodies in 22 patients with RW immunotherapy (IT) and in a different set of 31 patients, 16 of whom stopped RW IT after more than 5 years of treatment. Serum was assayed ...

    Abstract We studied the quantitative responses of short ragweed (RW)-pollen-specific serum antibodies in 22 patients with RW immunotherapy (IT) and in a different set of 31 patients, 16 of whom stopped RW IT after more than 5 years of treatment. Serum was assayed before and after season, 1 year before and 1 and 2 years after starting IT, and 1 year and 2 years after stopping IT. RW pan-IgG, RW IgG1, and RW IgG4 were measured by ELISA, and RW IgE by RAST. Absolute quantities of RW IgG1 and RW IgG4 in reference sera were estimated by least-squares multiple regression analysis of 223 sera with the equation RW pan-IgG = RW IgG1 + RW IgG4. IgG1 is dominant in the early immune response of IT and disappears relatively slowly when IT is stopped. In contrast, IgG4 appears in significant quantities only after prolonged IT and disappears rapidly when IT is stopped. The apparent average half-life of RW IgG4 (9 months) was significantly shorter than that of RW IgG1 (29 months) (p less than 0.001). Before IT, mean RW IgE rose 180% (p less than 0.01) during the RW pollination season (August to November). This seasonal rise in RW IgE was ablated after IT from 1 year up to 8 years, but returned the year after IT was stopped. After 2 years of IT, the RW IgG1 and IgG4 levels were significantly correlated with RW IgE (r = 0.94 and 0.81; p = 0.0001 and 0.005).
    MeSH term(s) Dose-Response Relationship, Immunologic ; Enzyme-Linked Immunosorbent Assay/methods ; Humans ; Immunoglobulin E/blood ; Immunoglobulin G/blood ; Immunotherapy/methods ; Pollen/immunology ; Radioallergosorbent Test/methods ; Rhinitis, Allergic, Seasonal/immunology ; Rhinitis, Allergic, Seasonal/therapy ; Skin Tests ; Time Factors
    Chemical Substances Immunoglobulin G ; Immunoglobulin E (37341-29-0)
    Language English
    Publishing date 1992-02
    Publishing country United States
    Document type Clinical Trial ; Comparative Study ; Journal Article ; Randomized Controlled Trial
    ZDB-ID 121011-7
    ISSN 1085-8725 ; 1097-6825 ; 0091-6749
    ISSN (online) 1085-8725 ; 1097-6825
    ISSN 0091-6749
    DOI 10.1016/0091-6749(92)90318-v
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Uh III Zs.92: Show issues Location:
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  7. Article: Association of protamine IgE and IgG antibodies with life-threatening reactions to intravenous protamine.

    Weiss, M E / Nyhan, D / Peng, Z K / Horrow, J C / Lowenstein, E / Hirshman, C / Adkinson, N F

    The New England journal of medicine

    1989  Volume 320, Issue 14, Page(s) 886–892

    Abstract: Life-threatening reactions to intravenous protamine, administered to reverse heparin anticoagulation, have been reported with increasing frequency as a consequence of the escalating use of cardiac catheterization and coronary bypass surgery. ... ...

    Abstract Life-threatening reactions to intravenous protamine, administered to reverse heparin anticoagulation, have been reported with increasing frequency as a consequence of the escalating use of cardiac catheterization and coronary bypass surgery. Retrospective studies have shown that such reactions are more common in diabetic patients receiving daily subcutaneous injections of protamine-insulin preparations. To determine whether anti-protamine IgE or IgG antibodies might explain the increased risk for protamine reactions among patients with protamine-insulin-dependent diabetes, we conducted a case-control study of 27 patients (diabetic and nondiabetic) who had acute reactions to intravenous protamine and 43 diabetic patients who tolerated protamine without a reaction during diagnostic or surgical procedures. Cases and controls were grouped according to previous exposure to protamine-insulin preparations. In diabetic patients who had received protamine-insulin injections, the presence of serum antiprotamine IgE antibody was a significant risk factor for acute protamine reactions (relative risk, 95; P = 1.0 X 10(-5), as was antiprotamine IgG (relative risk, 38; P = 1.2 X 10(-5). No patients without previous exposure to protamine-insulin injections had serum protamine IgE antibodies. In this group, anti-protamine IgG antibody was a risk factor for protamine reactions (relative risk, 25; P = 0.0062). We conclude that in protamine-insulin-dependent diabetics, the increased risk of serious reactions when intravenous protamine was given appeared to be caused largely by antibody-mediated mechanisms. In nondiabetic subjects, the presence of protamine IgG was significantly associated with an increased risk of acute protamine reactions, although many nondiabetic subjects who had reactions had no IgG antibodies.
    MeSH term(s) Adult ; Aged ; Aged, 80 and over ; Anaphylaxis/etiology ; Antibodies/analysis ; Diabetes Complications ; Diabetes Mellitus/drug therapy ; Drug Combinations ; Enzyme-Linked Immunosorbent Assay ; Female ; Humans ; Immunoglobulin E/analysis ; Immunoglobulin G/analysis ; Injections, Intravenous ; Insulin/administration & dosage ; Male ; Middle Aged ; Protamines/administration & dosage ; Protamines/adverse effects ; Protamines/immunology ; Radioallergosorbent Test
    Chemical Substances Antibodies ; Drug Combinations ; Immunoglobulin G ; Insulin ; Protamines ; Immunoglobulin E (37341-29-0)
    Language English
    Publishing date 1989-04-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 207154-x
    ISSN 1533-4406 ; 0028-4793
    ISSN (online) 1533-4406
    ISSN 0028-4793
    DOI 10.1056/NEJM198904063201402
    Database MEDical Literature Analysis and Retrieval System OnLINE

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