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  1. Article ; Online: Heterozygous IKKβ activation loop mutation results in a complex immunodeficiency syndrome.

    Abbott, Jordan / Ehler, Angelica C / Jayaraman, Divya / Reynolds, Paul R / Otsu, Kanao / Manka, Laurie / Gelfand, Erwin W

    The Journal of allergy and clinical immunology

    2020  Volume 147, Issue 2, Page(s) 737–740.e6

    MeSH term(s) Adult ; Bronchiectasis ; Fatal Outcome ; Hemorrhage ; Heterozygote ; Humans ; I-kappa B Kinase/genetics ; Immunologic Deficiency Syndromes/diagnosis ; Infections ; Lung/pathology ; Male ; Mutation/genetics ; Pedigree ; Protein Conformation ; Respiratory Insufficiency
    Chemical Substances I-kappa B Kinase (EC 2.7.11.10) ; IKBKB protein, human (EC 2.7.11.10)
    Language English
    Publishing date 2020-06-15
    Publishing country United States
    Document type Case Reports ; Letter ; Research Support, N.I.H., Extramural
    ZDB-ID 121011-7
    ISSN 1097-6825 ; 1085-8725 ; 0091-6749
    ISSN (online) 1097-6825 ; 1085-8725
    ISSN 0091-6749
    DOI 10.1016/j.jaci.2020.06.007
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Peanut allergy: an evolving clinical challenge.

    Otsu, Kanao / Dreskin, Stephen C

    Discovery medicine

    2011  Volume 12, Issue 65, Page(s) 319–328

    Abstract: Peanut allergy is an IgE-mediated food allergy responsible for causing severe and occasionally fatal reactions in those sensitized to peanuts. The prevalence of peanut allergy appears to be on the rise worldwide, yet there are no therapeutics currently ... ...

    Abstract Peanut allergy is an IgE-mediated food allergy responsible for causing severe and occasionally fatal reactions in those sensitized to peanuts. The prevalence of peanut allergy appears to be on the rise worldwide, yet there are no therapeutics currently available that can alter the course of this condition. This article will review the epidemiology, pathogenesis, and clinical features of peanut allergy and discuss future possibilities in diagnostic and therapeutic modalities.
    MeSH term(s) Arachis/immunology ; Humans ; Immunoglobulin E/immunology ; Peanut Hypersensitivity/drug therapy ; Peanut Hypersensitivity/epidemiology ; Peanut Hypersensitivity/immunology ; Peanut Hypersensitivity/pathology
    Chemical Substances Immunoglobulin E (37341-29-0)
    Language English
    Publishing date 2011-09-07
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2415544-5
    ISSN 1944-7930 ; 1944-7930
    ISSN (online) 1944-7930
    ISSN 1944-7930
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Therapeutics in food allergy: the current state of the art.

    Otsu, Kanao / Fleischer, David M

    Current allergy and asthma reports

    2011  Volume 12, Issue 1, Page(s) 48–54

    Abstract: Food allergy is an increasing public health dilemma in Westernized countries, yet no viable treatments are currently available for those who are afflicted. The only options available for patients with food allergies are prevention of reactions by strict ... ...

    Abstract Food allergy is an increasing public health dilemma in Westernized countries, yet no viable treatments are currently available for those who are afflicted. The only options available for patients with food allergies are prevention of reactions by strict avoidance of the offending food(s) and symptomatic treatment of any adverse effects from accidental exposures. Approaches are being pursued to develop treatments, and allergen-specific therapies such as oral immunotherapy, sublingual immunotherapy, and epicutaneous immunotherapy with different foods have shown promise. Other modalities are also being investigated, potentially leading to the discovery of novel therapeutic options.
    MeSH term(s) Administration, Oral ; Administration, Sublingual ; Allergens/administration & dosage ; Allergens/immunology ; Food Hypersensitivity/immunology ; Food Hypersensitivity/therapy ; Humans ; Immunomodulation ; Immunotherapy/methods ; Symptom Assessment/methods
    Chemical Substances Allergens
    Language English
    Publishing date 2011-11-19
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2057370-4
    ISSN 1534-6315 ; 1529-7322
    ISSN (online) 1534-6315
    ISSN 1529-7322
    DOI 10.1007/s11882-011-0235-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Mouse allergens in urban elementary schools and homes of children with asthma.

    Sheehan, William J / Rangsithienchai, Pitud A / Muilenberg, Michael L / Rogers, Christine A / Lane, Jeffrey P / Ghaemghami, Jalal / Rivard, Donald V / Otsu, Kanao / Hoffman, Elaine B / Israel, Elliot / Gold, Diane R / Phipatanakul, Wanda

    Annals of allergy, asthma & immunology : official publication of the American College of Allergy, Asthma, & Immunology

    2009  Volume 102, Issue 2, Page(s) 125–130

    Abstract: Background: The association between allergens in schools and childhood asthma has not been well studied, particularly in the United States.: Objective: To investigate allergen exposure in schools compared with homes with a specific focus on children ... ...

    Abstract Background: The association between allergens in schools and childhood asthma has not been well studied, particularly in the United States.
    Objective: To investigate allergen exposure in schools compared with homes with a specific focus on children with asthma.
    Methods: Dust samples were collected from 46 rooms in 4 urban elementary schools (northeastern United States) and from 38 student bedrooms. Samples were analyzed for cat (Fel d 1), dog (Can f 1), cockroach (Bla g 2), dust mites (Der f 1/Der p 1), and mouse urinary protein (MUP). Questionnaires identified students with physician-diagnosed asthma.
    Results: Cat and dog allergens were detectable in most school samples (96% and 78%, respectively), but at low levels. Cockroach allergen was detectable in only 11% of school samples. Mouse allergen was detectable in 89% of school samples, with 68% having MUP levels greater than 0.5 microg/g. In contrast, MUP was detectable in only 26% of bedroom samples. Matched classroom and home samples from 23 asthmatic students showed higher geometric mean MUP levels in the classroom vs the home (6.45 microg/g vs 0.44 microg/g, P < .001). However, there were lower geometric mean dust mite (Der f 1) levels in the classroom vs the home (0.04 microg/g vs 0.66 microg/g, P < .001).
    Conclusions: There are significantly higher levels of MUP but lower levels of Der f 1 in schools vs homes. It is important to recognize that children with asthma may encounter varying levels of allergens in environments outside the home, such as schools.
    MeSH term(s) Allergens/analysis ; Animals ; Antigens, Dermatophagoides/analysis ; Asthma/immunology ; Cats ; Child ; Cockroaches/immunology ; Dogs ; Dust ; Female ; Housing/statistics & numerical data ; Humans ; Male ; Mice ; Proteins/analysis ; Schools/statistics & numerical data ; United States
    Chemical Substances Allergens ; Antigens, Dermatophagoides ; Dust ; Proteins ; major urinary proteins
    Language English
    Publishing date 2009-02-18
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1228189-x
    ISSN 1534-4436 ; 1081-1206 ; 0003-4738
    ISSN (online) 1534-4436
    ISSN 1081-1206 ; 0003-4738
    DOI 10.1016/S1081-1206(10)60242-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase.

    Schumacher, Maria A / Bashor, Caleb J / Song, Minsun Hong / Otsu, Kanao / Zhu, Shuren / Parry, Ronald J / Ullman, Buddy / Brennan, Richard G

    Proceedings of the National Academy of Sciences of the United States of America

    2002  Volume 99, Issue 1, Page(s) 78–83

    Abstract: Uracil phosphoribosyltransferase (UPRT) is a member of a large family of salvage and biosynthetic enzymes, the phosphoribosyltransferases, and catalyzes the transfer of ribose 5-phosphate from alpha-d-5-phosphoribosyl-1-pyrophosphate (PRPP) to the N1 ... ...

    Abstract Uracil phosphoribosyltransferase (UPRT) is a member of a large family of salvage and biosynthetic enzymes, the phosphoribosyltransferases, and catalyzes the transfer of ribose 5-phosphate from alpha-d-5-phosphoribosyl-1-pyrophosphate (PRPP) to the N1 nitrogen of uracil. The UPRT from the opportunistic pathogen Toxoplasma gondii represents a promising target for rational drug design, because it can create intracellular, lethal nucleotides from subversive substrates. However, the development of such compounds requires a detailed understanding of the catalytic mechanism. Toward this end we determined the crystal structure of the T. gondii UPRT bound to uracil and cPRPP, a nonhydrolyzable PRPP analogue, to 2.5-A resolution. The structure suggests that the catalytic mechanism is substrate-assisted, and a tetramer would be the more active oligomeric form of the enzyme. Subsequent biochemical studies revealed that GTP binding, which has been suggested to play a role in catalysis by other UPRTs, causes a 6-fold activation of the T. gondii enzyme and strikingly stabilizes the tetramer form. The basis for stabilization was revealed in the 2.45-A resolution structure of the UPRT-GTP complex, whereby residues from three subunits contributed to GTP binding. Thus, our studies reveal an allosteric mechanism involving nucleotide stabilization of a more active, higher order oligomer. Such regulation of UPRT could play a role in the balance of purine and pyrimidine nucleotide pools in the cell.
    MeSH term(s) Animals ; Catalysis ; Dimerization ; Guanosine Triphosphate/chemistry ; Guanosine Triphosphate/metabolism ; Kinetics ; Ligands ; Light ; Models, Chemical ; Models, Molecular ; Mutagenesis, Site-Directed ; Pentosyltransferases/chemistry ; Protein Binding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Scattering, Radiation ; Substrate Specificity ; Toxoplasma/enzymology ; Uracil/chemistry
    Chemical Substances Ligands ; Uracil (56HH86ZVCT) ; Guanosine Triphosphate (86-01-1) ; Pentosyltransferases (EC 2.4.2.-) ; uracil phosphoribosyltransferase (EC 2.4.2.9)
    Language English
    Publishing date 2002-01-02
    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 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.012399599
    Database MEDical Literature Analysis and Retrieval System OnLINE

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