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  1. Article: Having found the unexpected, we should look again: in favor of lung cancer screening.

    Kolade, Victor O / Bosu, Dimple R

    Tennessee medicine : journal of the Tennessee Medical Association

    2014  Volume 107, Issue 2, Page(s) 37–38

    Abstract: Lung cancer is a leading cause of morbidity and death in the United States. A 65-year-old female with a 30 pack-year smoking history who requested screening for lung cancer was initially turned down in the absence of screening guidelines. Computed ... ...

    Abstract Lung cancer is a leading cause of morbidity and death in the United States. A 65-year-old female with a 30 pack-year smoking history who requested screening for lung cancer was initially turned down in the absence of screening guidelines. Computed tomography ordered a month later after review of current evidence revealed a 3.9-cm right lower lobe speculated mass proven to be adenocarcinoma on biopsy. Reflecting on this case, we concur with emerging national guidelines that patients who meet the selection criteria for the National Lung Screening Trial should be screened with annual Low Dose Computed Tomography.
    MeSH term(s) Adenocarcinoma/diagnostic imaging ; Aged ; Early Detection of Cancer/methods ; Female ; Humans ; Lung Neoplasms/diagnostic imaging ; Practice Guidelines as Topic ; Risk Factors ; Smoking ; Tomography, X-Ray Computed
    Language English
    Publishing date 2014-02
    Publishing country United States
    Document type Case Reports ; Journal Article
    ZDB-ID 1328497-6
    ISSN 1088-6222 ; 0040-3318
    ISSN 1088-6222 ; 0040-3318
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Cullin-RING ubiquitin ligases: global regulation and activation cycles.

    Bosu, Dimple R / Kipreos, Edward T

    Cell division

    2008  Volume 3, Page(s) 7

    Abstract: Cullin-RING ubiquitin ligases (CRLs) comprise the largest known category of ubiquitin ligases. CRLs regulate an extensive number of dynamic cellular processes, including multiple aspects of the cell cycle, transcription, signal transduction, and ... ...

    Abstract Cullin-RING ubiquitin ligases (CRLs) comprise the largest known category of ubiquitin ligases. CRLs regulate an extensive number of dynamic cellular processes, including multiple aspects of the cell cycle, transcription, signal transduction, and development. CRLs are multisubunit complexes composed of a cullin, RING H2 finger protein, a variable substrate-recognition subunit (SRS), and for most CRLs, an adaptor that links the SRS to the complex. Eukaryotic species contain multiple cullins, with five major types in metazoa. Each cullin forms a distinct class of CRL complex, with distinct adaptors and/or substrate-recognition subunits. Despite this diversity, each of the classes of CRL complexes is subject to similar regulatory mechanisms. This review focuses on the global regulation of CRL complexes, encompassing: neddylation, deneddylation by the COP9 Signalosome (CSN), inhibitory binding by CAND1, and the dimerization of CRL complexes. We also address the role of cycles of activation and inactivation in regulating CRL activity and switching between substrate-recognition subunits.
    Language English
    Publishing date 2008-02-18
    Publishing country England
    Document type Journal Article
    ISSN 1747-1028
    ISSN (online) 1747-1028
    DOI 10.1186/1747-1028-3-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Cullin-RING ubiquitin ligases

    Kipreos Edward T / Bosu Dimple R

    Cell Division, Vol 3, Iss 1, p

    global regulation and activation cycles

    2008  Volume 7

    Abstract: Abstract Cullin-RING ubiquitin ligases (CRLs) comprise the largest known category of ubiquitin ligases. CRLs regulate an extensive number of dynamic cellular processes, including multiple aspects of the cell cycle, transcription, signal transduction, and ...

    Abstract Abstract Cullin-RING ubiquitin ligases (CRLs) comprise the largest known category of ubiquitin ligases. CRLs regulate an extensive number of dynamic cellular processes, including multiple aspects of the cell cycle, transcription, signal transduction, and development. CRLs are multisubunit complexes composed of a cullin, RING H2 finger protein, a variable substrate-recognition subunit (SRS), and for most CRLs, an adaptor that links the SRS to the complex. Eukaryotic species contain multiple cullins, with five major types in metazoa. Each cullin forms a distinct class of CRL complex, with distinct adaptors and/or substrate-recognition subunits. Despite this diversity, each of the classes of CRL complexes is subject to similar regulatory mechanisms. This review focuses on the global regulation of CRL complexes, encompassing: neddylation, deneddylation by the COP9 Signalosome (CSN), inhibitory binding by CAND1, and the dimerization of CRL complexes. We also address the role of cycles of activation and inactivation in regulating CRL activity and switching between substrate-recognition subunits.
    Keywords Cytology ; QH573-671 ; Biology (General) ; QH301-705.5 ; Science ; Q ; DOAJ:Cytology ; DOAJ:Biology ; DOAJ:Biology and Life Sciences
    Subject code 571
    Language English
    Publishing date 2008-02-01T00:00:00Z
    Publisher BioMed Central
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: C. elegans CAND-1 regulates cullin neddylation, cell proliferation and morphogenesis in specific tissues.

    Bosu, Dimple R / Feng, Hui / Min, Kyoengwoo / Kim, Youngjo / Wallenfang, Matthew R / Kipreos, Edward T

    Developmental biology

    2010  Volume 346, Issue 1, Page(s) 113–126

    Abstract: Cullin-RING ubiquitin ligases (CRLs) are critical regulators of multiple developmental and cellular processes in eukaryotes. CAND1 is a biochemical inhibitor of CRLs, yet has been shown to promote CRL activity in plant and mammalian cells. Here we ... ...

    Abstract Cullin-RING ubiquitin ligases (CRLs) are critical regulators of multiple developmental and cellular processes in eukaryotes. CAND1 is a biochemical inhibitor of CRLs, yet has been shown to promote CRL activity in plant and mammalian cells. Here we analyze CAND1 function in the context of a developing metazoan organism. Caenorhabditis elegans CAND-1 is capable of binding to all of the cullins, and we show that it physically interacts with CUL-2 and CUL-4 in vivo. The covalent attachment of the ubiquitin-like protein Nedd8 is required for cullin activity in animals and plants. In cand-1 mutants, the levels of the neddylated isoforms of CUL-2 and CUL-4 are increased, indicating that CAND-1 is a negative regulator of cullin neddylation. cand-1 mutants are hypersensitive to the partial loss of cullin activity, suggesting that CAND-1 facilitates CRL functions. cand-1 mutants exhibit impenetrant phenotypes, including developmental arrest, morphological defects of the vulva and tail, and reduced fecundity. cand-1 mutants share with cul-1 and lin-23 mutants the phenotypes of supernumerary seam cell divisions, defective alae formation, and the accumulation of the SCF(LIN-23) target the glutamate receptor GLR-1. The observation that cand-1 mutants have phenotypes associated with the loss of the SCF(LIN-23) complex, but lack phenotypes associated with other specific CRL complexes, suggests that CAND-1 is differentially required for the activity of distinct CRL complexes.
    MeSH term(s) Animals ; Caenorhabditis elegans/embryology ; Caenorhabditis elegans Proteins/analysis ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Caenorhabditis elegans Proteins/physiology ; Carrier Proteins/analysis ; Carrier Proteins/genetics ; Carrier Proteins/physiology ; Cell Cycle Proteins/metabolism ; Cell Proliferation ; Cullin Proteins/genetics ; Cullin Proteins/metabolism ; F-Box Proteins/metabolism ; Ligases/genetics ; Ligases/metabolism ; Morphogenesis ; Mutation ; Phenotype ; Protein Isoforms ; Ubiquitin-Protein Ligases/physiology
    Chemical Substances CAND-1 protein, C elegans ; Caenorhabditis elegans Proteins ; Carrier Proteins ; Cell Cycle Proteins ; Cul-4 protein, C elegans ; Cullin Proteins ; F-Box Proteins ; Protein Isoforms ; cul-2 proteins, C elegans ; lin-23 protein, C elegans ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Ligases (EC 6.-)
    Language English
    Publishing date 2010-07-24
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1114-9
    ISSN 1095-564X ; 0012-1606
    ISSN (online) 1095-564X
    ISSN 0012-1606
    DOI 10.1016/j.ydbio.2010.07.020
    Database MEDical Literature Analysis and Retrieval System OnLINE

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