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  1. Book: Anticancer drugs

    Powis, Garth

    reactive metabolism and drug interactions

    (International encyclopedia of pharmacology and therapeutics ; 141)

    1994  

    Author's details specialist subject ed. Garth Powis
    Series title International encyclopedia of pharmacology and therapeutics ; 141
    Collection
    Keywords Antineoplastic Agents / metabolism ; Drug Interactions
    Language English
    Size XV, 444 S. : Ill., graph. Darst.
    Edition 1. ed.
    Publisher Pergamon Press
    Publishing place Oxford u.a.
    Publishing country Great Britain
    Document type Book
    HBZ-ID HT006204433
    ISBN 0-08-042335-3 ; 978-0-08-042335-7
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    1994 A 1367 order for loan Magazin

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  2. Book: Anticancer drugs

    Powis, Garth

    antimetabolite metabolism and natural anticancer agents

    (International encyclopedia of pharmacology and therapeutics ; 140)

    1994  

    Author's details specialist subject ed. Garth Powis
    Series title International encyclopedia of pharmacology and therapeutics ; 140
    Collection
    Keywords Antineoplastic Agents ; Antineoplastic Agents, Phytogenic ; Antimetabolites, Antineoplastic
    Language English
    Size XVIII, 506 S. : Ill., graph. Darst.
    Edition 1. ed.
    Publisher Pergamon Press
    Publishing place Oxford u.a.
    Publishing country Great Britain
    Document type Book
    HBZ-ID HT006408589
    ISBN 0-08-042334-5 ; 978-0-08-042334-0
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    1994 A 3787 order for loan Magazin

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  3. Book: The toxicity of anticancer drugs

    Powis, Garth

    1991  

    Author's details ed. by Garth Powis
    Keywords Antineoplastic Agents / toxicity ; Cytostatikum ; Toxizität ; Arzneimittelnebenwirkung
    Subject Arzneimittel ; Unerwünschte Arzneimittelwirkung ; UAW ; Zytostatikum ; Cancerotoxischer Stoff ; Carcinostatikum ; Krebsmittel ; Antineoplastikum ; Anticarcinogen ; Antikarzinogen ; Anticancerogen ; Antineoplastisches Mittel ; Giftigkeit ; Toxische Wirkung
    Size IX, 228 S. : graph. Darst.
    Edition 1. print
    Publisher Pergamon Pr
    Publishing place New York u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT003895300
    ISBN 0-08-040302-6 ; 978-0-08-040302-1
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    1991 A 4565 order for loan Magazin

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  4. Article ; Online: Pleckstrin Homology [PH] domain, structure, mechanism, and contribution to human disease.

    Powis, Garth / Meuillet, Emmanuelle J / Indarte, Martin / Booher, Garrett / Kirkpatrick, Lynn

    Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie

    2023  Volume 165, Page(s) 115024

    Abstract: The pleckstrin homology [PH] domain is a structural fold found in more than 250 proteins making it the 11th most common domain in the human proteome. 25% of family members have more than one PH domain and some PH domains are split by one, or several ... ...

    Abstract The pleckstrin homology [PH] domain is a structural fold found in more than 250 proteins making it the 11th most common domain in the human proteome. 25% of family members have more than one PH domain and some PH domains are split by one, or several other, protein domains although still folding to give functioning PH domains. We review mechanisms of PH domain activity, the role PH domain mutation plays in human disease including cancer, hyperproliferation, neurodegeneration, inflammation, and infection, and discuss pharmacotherapeutic approaches to regulate PH domain activity for the treatment of human disease. Almost half PH domain family members bind phosphatidylinositols [PIs] that attach the host protein to cell membranes where they interact with other membrane proteins to give signaling complexes or cytoskeleton scaffold platforms. A PH domain in its native state may fold over other protein domains thereby preventing substrate access to a catalytic site or binding with other proteins. The resulting autoinhibition can be released by PI binding to the PH domain, or by protein phosphorylation thus providing fine tuning of the cellular control of PH domain protein activity. For many years the PH domain was thought to be undruggable until high-resolution structures of human PH domains allowed structure-based design of novel inhibitors that selectively bind the PH domain. Allosteric inhibitors of the Akt1 PH domain have already been tested in cancer patients and for proteus syndrome, with several other PH domain inhibitors in preclinical development for treatment of other human diseases.
    MeSH term(s) Humans ; Pleckstrin Homology Domains ; Binding Sites ; Blood Proteins/metabolism ; Phosphoproteins/metabolism ; Protein Binding
    Chemical Substances platelet protein P47 ; Blood Proteins ; Phosphoproteins
    Language English
    Publishing date 2023-07-01
    Publishing country France
    Document type Journal Article ; Review
    ZDB-ID 392415-4
    ISSN 1950-6007 ; 0753-3322 ; 0300-0893
    ISSN (online) 1950-6007
    ISSN 0753-3322 ; 0300-0893
    DOI 10.1016/j.biopha.2023.115024
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Book: Metabolism and action of anti-cancer drugs

    Powis, Garth

    1987  

    Author's details ed. by Garth Powis
    Keywords Antineoplastic Agents / metabolism ; Antineoplastic Agents / pharmacology ; Cytostatikum ; Pharmakodynamik ; Stoffwechsel
    Subject Metabolismus ; Verstoffwechselung ; Metabolische Regulation ; Zytostatikum ; Cancerotoxischer Stoff ; Carcinostatikum ; Krebsmittel ; Antineoplastikum ; Anticarcinogen ; Antikarzinogen ; Anticancerogen ; Antineoplastisches Mittel
    Language English
    Size XV, 336 S. : graph. Darst.
    Publisher Taylor & Francis
    Publishing place London u.a.
    Publishing country Great Britain
    Document type Book
    HBZ-ID HT003116182
    ISBN 0-85066-369-5 ; 978-0-85066-369-3
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    1988 A 2414 order for loan Magazin

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  6. Article ; Online: Clinically Evaluated Cancer Drugs Inhibiting Redox Signaling.

    Kirkpatrick, D Lynn / Powis, Garth

    Antioxidants & redox signaling

    2017  Volume 26, Issue 6, Page(s) 262–273

    Abstract: Significance: There are a number of redox-active anticancer agents currently in development based on the premise that altered redox homeostasis is necessary for cancer cell's survival. Recent Advances: This review focuses on the relatively few agents ... ...

    Abstract Significance: There are a number of redox-active anticancer agents currently in development based on the premise that altered redox homeostasis is necessary for cancer cell's survival. Recent Advances: This review focuses on the relatively few agents that target cellular redox homeostasis to have entered clinical trial as anticancer drugs.
    Critical issues: The success rate of redox anticancer drugs has been disappointing compared to other classes of anticancer agents. This is due, in part, to our incomplete understanding of the functions of the redox targets in normal and cancer tissues, leading to off-target toxicities and low therapeutic indexes of the drugs. The field also lags behind in the use biomarkers and other means to select patients who are most likely to respond to redox-targeted therapy.
    Future directions: If we wish to derive clinical benefit from agents that attack redox targets, then the future will require a more sophisticated understanding of the role of redox targets in cancer and the increased application of personalized medicine principles for their use. Antioxid. Redox Signal. 26, 262-273.
    MeSH term(s) Animals ; Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Biomarkers ; Homeostasis/drug effects ; Humans ; Mitochondria/drug effects ; Mitochondria/metabolism ; Molecular Targeted Therapy ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Neoplasms/pathology ; Oxidation-Reduction/drug effects ; Reactive Oxygen Species/antagonists & inhibitors ; Reactive Oxygen Species/metabolism ; Signal Transduction/drug effects ; Treatment Outcome
    Chemical Substances Antineoplastic Agents ; Biomarkers ; Reactive Oxygen Species
    Language English
    Publishing date 2017-02-20
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 1483836-9
    ISSN 1557-7716 ; 1523-0864
    ISSN (online) 1557-7716
    ISSN 1523-0864
    DOI 10.1089/ars.2016.6633
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 5488: Show issues Location:
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  7. Article: Achieving personalized cancer medicine: trials and tribulations.

    Powis, Garth

    Journal of investigative medicine : the official publication of the American Federation for Clinical Research

    2006  Volume 54, Issue 5, Page(s) 235–237

    MeSH term(s) Drug Therapy/methods ; Genotype ; Humans ; Neoplasms/drug therapy ; Personal Health Services ; Pharmacogenetics
    Language English
    Publishing date 2006-07
    Publishing country England
    Document type Journal Article
    ZDB-ID 1217870-6
    ISSN 1708-8267 ; 1081-5589 ; 0009-9279
    ISSN (online) 1708-8267
    ISSN 1081-5589 ; 0009-9279
    DOI 10.2310/6650.2006.06026
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 307: Show issues Location:
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  8. Article: Passing the baton: the HIF switch.

    Koh, Mei Yee / Powis, Garth

    Trends in biochemical sciences

    2012  Volume 37, Issue 9, Page(s) 364–372

    Abstract: Hypoxia is an inadequate oxygen supply to tissues and cells, which can restrict their function. The hypoxic response is primarily mediated by the hypoxia-inducible transcription factors, HIF-1 and HIF-2, which have both overlapping and unique target ... ...

    Abstract Hypoxia is an inadequate oxygen supply to tissues and cells, which can restrict their function. The hypoxic response is primarily mediated by the hypoxia-inducible transcription factors, HIF-1 and HIF-2, which have both overlapping and unique target genes. HIF target gene activation is highly context specific and is not a reliable indicator of which HIF-α isoform is active. For example, in some cell lines, the individual HIFs have specific temporal and functional roles: HIF-1 drives the initial response to hypoxia (<24h) and HIF-2 drives the chronic response (>24h). Here, we review the significance of the HIF switch and the relation between HIF-1 and HIF-2 under both physiological and pathophysiological conditions.
    MeSH term(s) Animals ; Basic Helix-Loop-Helix Transcription Factors/metabolism ; Cell Hypoxia ; Humans ; Hypoxia/metabolism ; Oxygen/metabolism ; Stem Cells/metabolism ; Transcriptional Activation
    Chemical Substances Basic Helix-Loop-Helix Transcription Factors ; Oxygen (S88TT14065)
    Language English
    Publishing date 2012-07-18
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 194216-5
    ISSN 1362-4326 ; 0968-0004 ; 0376-5067
    ISSN (online) 1362-4326
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2012.06.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1207: Show issues Location:
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  9. Article ; Online: A Robust and Cost-Effective Luminescent-Based High-Throughput Assay for Fructose-1,6-Bisphosphate Aldolase A.

    Cho, Eun Jeong / Devkota, Ashwini K / Stancu, Gabriel / Edupunganti, Ramakrishna / Debevec, Ginamarie / Giulianotti, Marc / Houghten, Richard / Powis, Garth / Dalby, Kevin N

    SLAS discovery : advancing life sciences R & D

    2020  Volume 25, Issue 9, Page(s) 1038–1046

    Abstract: Hypoxic solid tumors induce the stabilization of hypoxia-inducible factor 1 alpha (HIF1α), which stimulates the expression of many glycolytic enzymes and hypoxia-responsive genes. A high rate of glycolysis supports the energetic and material needs for ... ...

    Abstract Hypoxic solid tumors induce the stabilization of hypoxia-inducible factor 1 alpha (HIF1α), which stimulates the expression of many glycolytic enzymes and hypoxia-responsive genes. A high rate of glycolysis supports the energetic and material needs for tumors to grow. Fructose-1,6-bisphosphate aldolase A (ALDOA) is an enzyme in the glycolytic pathway that promotes the expression of HIF1α. Therefore, inhibition of ALDOA activity represents a potential therapeutic approach for a range of cancers by blocking two critical cancer survival mechanisms. Here, we present a luminescence-based strategy to determine ALDOA activity. The assay platform was developed by integrating a previously established ALDOA activity assay with a commercial NAD/NADH detection kit, resulting in a significant (>12-fold) improvement in signal/background (S/B) compared with previous assay platforms. A screening campaign using a mixture-based compound library exhibited excellent statistical parameters of Z' (>0.8) and S/B (~20), confirming its robustness and readiness for high-throughput screening (HTS) application. This assay platform provides a cost-effective method for identifying ALDOA inhibitors using a large-scale HTS campaign.
    MeSH term(s) Cost-Benefit Analysis ; Fructose/genetics ; Fructose/metabolism ; Fructose-Bisphosphate Aldolase/genetics ; Fructose-Bisphosphate Aldolase/isolation & purification ; Glycolysis/genetics ; High-Throughput Screening Assays ; Humans ; Hypoxia-Inducible Factor 1, alpha Subunit/genetics ; Luminescence
    Chemical Substances HIF1A protein, human ; Hypoxia-Inducible Factor 1, alpha Subunit ; Fructose (30237-26-4) ; ALDOA protein, human (EC 4.1.2.13) ; Fructose-Bisphosphate Aldolase (EC 4.1.2.13)
    Language English
    Publishing date 2020-05-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2885123-7
    ISSN 2472-5560 ; 2472-5552
    ISSN (online) 2472-5560
    ISSN 2472-5552
    DOI 10.1177/2472555220926146
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 4911: Show issues Location:
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  10. Article ; Online: Structural basis for the association of PLEKHA7 with membrane-embedded phosphatidylinositol lipids.

    Aleshin, Alexander E / Yao, Yong / Iftikhar, Amer / Bobkov, Andrey A / Yu, Jinghua / Cadwell, Gregory / Klein, Michael G / Dong, Chuqiao / Bankston, Laurie A / Liddington, Robert C / Im, Wonpil / Powis, Garth / Marassi, Francesca M

    Structure (London, England : 1993)

    2021  Volume 29, Issue 9, Page(s) 1029–1039.e3

    Abstract: PLEKHA7 (pleckstrin homology domain containing family A member 7) plays key roles in intracellular signaling, cytoskeletal organization, and cell adhesion, and is associated with multiple human cancers. The interactions of its pleckstrin homology (PH) ... ...

    Abstract PLEKHA7 (pleckstrin homology domain containing family A member 7) plays key roles in intracellular signaling, cytoskeletal organization, and cell adhesion, and is associated with multiple human cancers. The interactions of its pleckstrin homology (PH) domain with membrane phosphatidyl-inositol-phosphate (PIP) lipids are critical for proper cellular localization and function, but little is known about how PLEKHA7 and other PH domains interact with membrane-embedded PIPs. Here we describe the structural basis for recognition of membrane-bound PIPs by PLEHA7. Using X-ray crystallography, nuclear magnetic resonance, molecular dynamics simulations, and isothermal titration calorimetry, we show that the interaction of PLEKHA7 with PIPs is multivalent, distinct from a discrete one-to-one interaction, and induces PIP clustering. Our findings reveal a central role of the membrane assembly in mediating protein-PIP association and provide a roadmap for understanding how the PH domain contributes to the signaling, adhesion, and nanoclustering functions of PLEKHA7.
    MeSH term(s) Binding Sites ; Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Humans ; Lipid Bilayers/chemistry ; Lipid Bilayers/metabolism ; Phosphatidylinositols/chemistry ; Phosphatidylinositols/metabolism ; Protein Binding
    Chemical Substances Carrier Proteins ; Lipid Bilayers ; PLEKHA7 protein, human ; Phosphatidylinositols
    Language English
    Publishing date 2021-04-19
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2021.03.018
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 4141: Show issues Location:
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