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  1. Artikel: Transfusion-related acute lung injury: past, present, and future.

    Cherry, Tad / Steciuk, Mark / Reddy, Vishnu V B / Marques, Marisa B

    American journal of clinical pathology

    2008  Band 129, Heft 2, Seite(n) 287–297

    Abstract: Noncardiogenic pulmonary edema caused by transfusion has been observed for almost 60 years. Today, we know this entity as transfusion-related acute lung injury (TRALI). TRALI is an uncommon but potentially fatal adverse reaction to transfusion of plasma- ... ...

    Abstract Noncardiogenic pulmonary edema caused by transfusion has been observed for almost 60 years. Today, we know this entity as transfusion-related acute lung injury (TRALI). TRALI is an uncommon but potentially fatal adverse reaction to transfusion of plasma-containing blood components. It is typified by dyspnea, cough, hypoxemia, and pulmonary edema within 6 hours of transfusion. Most commonly, it is caused by donor HLA antibodies that react with recipient antigens. It may also be caused by biologically active compounds accumulated during storage of blood products, which are capable of priming neutrophils. Without a "gold standard," the diagnosis of TRALI relies on a high index of suspicion and on excluding other types of transfusion reactions. Although current definitions of TRALI depend on symptoms, laboratory parameters can aid in the diagnosis and frequently identify the causative donor unit. As our understanding of TRALI deepens, risk reduction or prevention may become possible.
    Mesh-Begriff(e) Blood Component Transfusion/adverse effects ; Forecasting ; HLA Antigens/immunology ; Humans ; Lung Diseases/diagnosis ; Lung Diseases/etiology ; Pulmonary Edema/etiology ; Respiratory Distress Syndrome, Adult/etiology ; Transfusion Reaction
    Chemische Substanzen HLA Antigens
    Sprache Englisch
    Erscheinungsdatum 2008-02
    Erscheinungsland England
    Dokumenttyp Journal Article ; Review
    ZDB-ID 2944-0
    ISSN 1943-7722 ; 0002-9173
    ISSN (online) 1943-7722
    ISSN 0002-9173
    DOI 10.1309/D3F7BXH466AE3G0P
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Structural insights into interactions of C/EBP transcriptional activators with the Taz2 domain of p300.

    Bhaumik, Prasenjit / Davis, Jamaine / Tropea, Joseph E / Cherry, Scott / Johnson, Peter F / Miller, Maria

    Acta crystallographica. Section D, Biological crystallography

    2014  Band 70, Heft Pt 7, Seite(n) 1914–1921

    Abstract: ... to the C/EBPℇ TAD forms two orthogonally disposed helices connected by a short linker and interacts ... homology boxes A and B, which comprise their minimal transactivation domains (TADs), are conserved between ... between C/EBP TADs and the p300 Taz2 domain was implied by the crystal structure of a chimeric protein ...

    Abstract Members of the C/EBP family of transcription factors bind to the Taz2 domain of p300/CBP and mediate its phosphorylation through the recruitment of specific kinases. Short sequence motifs termed homology boxes A and B, which comprise their minimal transactivation domains (TADs), are conserved between C/EBP activators and are necessary for specific p300/CBP binding. A possible mode of interaction between C/EBP TADs and the p300 Taz2 domain was implied by the crystal structure of a chimeric protein composed of residues 1723-1818 of p300 Taz2 and residues 37-61 of C/EBPℇ. The segment corresponding to the C/EBPℇ TAD forms two orthogonally disposed helices connected by a short linker and interacts with the core structure of Taz2 from a symmetry-related molecule. It is proposed that other members of the C/EBP family interact with the Taz2 domain in the same manner. The position of the C/EBPℇ peptide on the Taz2 protein interaction surface suggests that the N-termini of C/EBP proteins are unbound in the C/EBP-p300 Taz2 complex. This observation is in agreement with the known location of the docking site of protein kinase HIPK2 in the C/EBPβ N-terminus, which associates with the C/EBPβ-p300 complex.
    Mesh-Begriff(e) Amino Acid Sequence ; CCAAT-Enhancer-Binding Proteins/chemistry ; CCAAT-Enhancer-Binding Proteins/metabolism ; Crystallography, X-Ray ; Molecular Sequence Data ; Phosphorylation ; Protein Conformation ; Sequence Homology, Amino Acid ; p300-CBP Transcription Factors/chemistry
    Chemische Substanzen CCAAT-Enhancer-Binding Proteins ; p300-CBP Transcription Factors (EC 2.3.1.48)
    Sprache Englisch
    Erscheinungsdatum 2014-06-29
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 2020492-9
    ISSN 1399-0047 ; 0907-4449
    ISSN (online) 1399-0047
    ISSN 0907-4449
    DOI 10.1107/S1399004714009262
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Structure of the Taz2 domain of p300: insights into ligand binding.

    Miller, Maria / Dauter, Zbigniew / Cherry, Scott / Tropea, Joseph E / Wlodawer, Alexander

    Acta crystallographica. Section D, Biological crystallography

    2009  Band 65, Heft Pt 12, Seite(n) 1301–1308

    Abstract: ... of the recognition of diverse transactivation domains (TADs) by Taz2. On the basis of these results and ...

    Abstract CBP and its paralog p300 are histone acetyl transferases that regulate gene expression by interacting with multiple transcription factors via specialized domains. The structure of a segment of human p300 protein (residues 1723-1836) corresponding to the extended zinc-binding Taz2 domain has been investigated. The crystal structure was solved by the SAD approach utilizing the anomalous diffraction signal of the bound Zn ions. The structure comprises an atypical helical bundle stabilized by three Zn ions and closely resembles the solution structures determined previously for shorter peptides. Residues 1813-1834 from the current construct form a helical extension of the C-terminal helix and make extensive crystal-contact interactions with the peptide-binding site of Taz2, providing additional insights into the mechanism of the recognition of diverse transactivation domains (TADs) by Taz2. On the basis of these results and molecular modeling, a hypothetical model of the binding of phosphorylated p53 TAD1 to Taz2 has been proposed.
    Mesh-Begriff(e) Amino Acid Sequence ; Crystallography, X-Ray ; E1A-Associated p300 Protein/chemistry ; E1A-Associated p300 Protein/metabolism ; Humans ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Interaction Domains and Motifs
    Chemische Substanzen Ligands ; E1A-Associated p300 Protein (EC 2.3.1.48) ; EP300 protein, human (EC 2.3.1.48)
    Sprache Englisch
    Erscheinungsdatum 2009-11-17
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Intramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2020492-9
    ISSN 1399-0047 ; 0907-4449
    ISSN (online) 1399-0047
    ISSN 0907-4449
    DOI 10.1107/S0907444909040153
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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