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  1. Article ; Online: SARAH Domain-Mediated MST2-RASSF Dimeric Interactions.

    Sánchez-Sanz, Goar / Tywoniuk, Bartłomiej / Matallanas, David / Romano, David / Nguyen, Lan K / Kholodenko, Boris N / Rosta, Edina / Kolch, Walter / Buchete, Nicolae-Viorel

    PLoS computational biology

    2016  Volume 12, Issue 10, Page(s) e1005051

    Abstract: ... The regulation of MST1/2 includes both homo- and heterodimerization, mediated by helical SARAH domains ... RASSF5, and MST2 SARAH domains by using both atomistic molecular simulation techniques and experiments ... We construct and study models of MST2 homodimers and MST2-RASSF SARAH heterodimers, and we identify the factors ...

    Abstract RASSF enzymes act as key apoptosis activators and tumor suppressors, being downregulated in many human cancers, although their exact regulatory roles remain unknown. A key downstream event in the RASSF pathway is the regulation of MST kinases, which are main effectors of RASSF-induced apoptosis. The regulation of MST1/2 includes both homo- and heterodimerization, mediated by helical SARAH domains, though the underlying molecular interaction mechanism is unclear. Here, we study the interactions between RASSF1A, RASSF5, and MST2 SARAH domains by using both atomistic molecular simulation techniques and experiments. We construct and study models of MST2 homodimers and MST2-RASSF SARAH heterodimers, and we identify the factors that control their high molecular stability. In addition, we also analyze both computationally and experimentally the interactions of MST2 SARAH domains with a series of synthetic peptides particularly designed to bind to it, and hope that our approach can be used to address some of the challenging problems in designing new anti-cancer drugs.
    MeSH term(s) Binding Sites ; Carrier Proteins/chemistry ; Carrier Proteins/ultrastructure ; Cyclin-Dependent Kinase Inhibitor p15/chemistry ; Cyclin-Dependent Kinase Inhibitor p15/ultrastructure ; Dimerization ; Drosophila Proteins/chemistry ; Drosophila Proteins/ultrastructure ; Enzyme Activation ; Molecular Docking Simulation ; Protein Binding ; Protein Conformation ; Protein Domains
    Chemical Substances CDKN2B protein, human ; Carrier Proteins ; Cyclin-Dependent Kinase Inhibitor p15 ; Drosophila Proteins ; RASSF protein, Drosophila
    Language English
    Publishing date 2016-10
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2193340-6
    ISSN 1553-7358 ; 1553-734X
    ISSN (online) 1553-7358
    ISSN 1553-734X
    DOI 10.1371/journal.pcbi.1005051
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: MST2-RASSF protein-protein interactions through SARAH domains.

    Sánchez-Sanz, Goar / Matallanas, David / Nguyen, Lan K / Kholodenko, Boris N / Rosta, Edina / Kolch, Walter / Buchete, Nicolae-Viorel

    Briefings in bioinformatics

    2016  Volume 17, Issue 4, Page(s) 593–602

    Abstract: ... being played by the specific interactions between the helical Salvador/RASSF/Hippo (SARAH) domains ...

    Abstract The detailed, atomistic-level understanding of molecular signaling along the tumor-suppressive Hippo signaling pathway that controls tissue homeostasis by balancing cell proliferation and death through apoptosis is a promising avenue for the discovery of novel anticancer drug targets. The activation of kinases such as Mammalian STE20-Like Protein Kinases 1 and 2 (MST1 and MST2)-modulated through both homo- and heterodimerization (e.g. interactions with Ras association domain family, RASSF, enzymes)-is a key upstream event in this pathway and remains poorly understood. On the other hand, RASSFs (such as RASSF1A or RASSF5) act as important apoptosis activators and tumor suppressors, although their exact regulatory roles are also unclear. We present recent molecular studies of signaling along the Ras-RASSF-MST pathway, which controls growth and apoptosis in eukaryotic cells, including a variety of modern molecular modeling and simulation techniques. Using recently available structural information, we discuss the complex regulatory scenario according to which RASSFs perform dual signaling functions, either preventing or promoting MST2 activation, and thus control cell apoptosis. Here, we focus on recent studies highlighting the special role being played by the specific interactions between the helical Salvador/RASSF/Hippo (SARAH) domains of MST2 and RASSF1a or RASSF5 enzymes. These studies are crucial for integrating atomistic-level mechanistic information about the structures and conformational dynamics of interacting proteins, with information available on their system-level functions in cellular signaling.
    Language English
    Publishing date 2016-07
    Publishing country England
    Document type Journal Article
    ZDB-ID 2068142-2
    ISSN 1477-4054 ; 1467-5463
    ISSN (online) 1477-4054
    ISSN 1467-5463
    DOI 10.1093/bib/bbv070
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: SARAH Domain-Mediated MST2-RASSF Dimeric Interactions.

    Goar Sánchez-Sanz / Bartłomiej Tywoniuk / David Matallanas / David Romano / Lan K Nguyen / Boris N Kholodenko / Edina Rosta / Walter Kolch / Nicolae-Viorel Buchete

    PLoS Computational Biology, Vol 12, Iss 10, p e

    2016  Volume 1005051

    Abstract: ... The regulation of MST1/2 includes both homo- and heterodimerization, mediated by helical SARAH domains ... RASSF5, and MST2 SARAH domains by using both atomistic molecular simulation techniques and experiments ... We construct and study models of MST2 homodimers and MST2-RASSF SARAH heterodimers, and we identify the factors ...

    Abstract RASSF enzymes act as key apoptosis activators and tumor suppressors, being downregulated in many human cancers, although their exact regulatory roles remain unknown. A key downstream event in the RASSF pathway is the regulation of MST kinases, which are main effectors of RASSF-induced apoptosis. The regulation of MST1/2 includes both homo- and heterodimerization, mediated by helical SARAH domains, though the underlying molecular interaction mechanism is unclear. Here, we study the interactions between RASSF1A, RASSF5, and MST2 SARAH domains by using both atomistic molecular simulation techniques and experiments. We construct and study models of MST2 homodimers and MST2-RASSF SARAH heterodimers, and we identify the factors that control their high molecular stability. In addition, we also analyze both computationally and experimentally the interactions of MST2 SARAH domains with a series of synthetic peptides particularly designed to bind to it, and hope that our approach can be used to address some of the challenging problems in designing new anti-cancer drugs.
    Keywords Biology (General) ; QH301-705.5
    Language English
    Publishing date 2016-10-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article: MST2-RASSF protein–protein interactions through SARAH domains

    Sánchez-Sanz, Goar / Matallanas, David / Nguyen, Lan K / Kholodenko, Boris N / Rosta, Edina / Kolch, Walter / Buchete, Nicolae-Viorel

    Briefings in bioinformatics. 2016 July, v. 17, no. 4

    2016  

    Abstract: ... being played by the specific interactions between the helical Salvador/RASSF/Hippo (SARAH) domains ...

    Abstract The detailed, atomistic-level understanding of molecular signaling along the tumor-suppressive Hippo signaling pathway that controls tissue homeostasis by balancing cell proliferation and death through apoptosis is a promising avenue for the discovery of novel anticancer drug targets. The activation of kinases such as Mammalian STE20-Like Protein Kinases 1 and 2 (MST1 and MST2)—modulated through both homo- and heterodimerization (e.g. interactions with Ras association domain family, RASSF, enzymes)—is a key upstream event in this pathway and remains poorly understood. On the other hand, RASSFs (such as RASSF1A or RASSF5) act as important apoptosis activators and tumor suppressors, although their exact regulatory roles are also unclear. We present recent molecular studies of signaling along the Ras-RASSF-MST pathway, which controls growth and apoptosis in eukaryotic cells, including a variety of modern molecular modeling and simulation techniques. Using recently available structural information, we discuss the complex regulatory scenario according to which RASSFs perform dual signaling functions, either preventing or promoting MST2 activation, and thus control cell apoptosis. Here, we focus on recent studies highlighting the special role being played by the specific interactions between the helical Salvador/RASSF/Hippo (SARAH) domains of MST2 and RASSF1a or RASSF5 enzymes. These studies are crucial for integrating atomistic-level mechanistic information about the structures and conformational dynamics of interacting proteins, with information available on their system-level functions in cellular signaling.
    Keywords antineoplastic agents ; apoptosis ; cell proliferation ; death ; dimerization ; eukaryotic cells ; homeostasis ; mammals ; molecular models ; neoplasms ; protein kinases ; protein-protein interactions ; proteins ; signal transduction
    Language English
    Dates of publication 2016-07
    Size p. 593-602.
    Publishing place Oxford University Press
    Document type Article
    ZDB-ID 2068142-2
    ISSN 1477-4054 ; 1467-5463
    ISSN (online) 1477-4054
    ISSN 1467-5463
    DOI 10.1093/bib/bbv070
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6262: Show issues Location:
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  5. Book: Normdosen gebräuchlicher Arzneistoffe und Drogen

    Haffner, Felix / Schultz, Otto-Erich / Schmid, Walter / Braun, Rainer / Wessinger, Sarah

    2023  

    Author's details begründet von Felix Haffner, Otto-Erich Schultz und Walter Schmid und Rainer Braun; bearbeitet von Sarah Wessinger
    Keywords Arzneimitteldosis
    Subject Arzneimitteldosierung ; Dosierung ; Arzneimittel ; Normdosis
    Subject code 615.14
    Language German
    Size 1 Band (Loseblattausgabe), 24 cm
    Edition 28., aktualisierte und erweiterte Auflage
    Publisher Wissenschaftliche Verlagsgesellschaft
    Publishing place Stuttgart
    Publishing country Germany
    Document type Book
    HBZ-ID HT021481919
    ISBN 978-3-8047-4394-6 ; 3-8047-4394-3
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2024 A 2 available for loan (reading room) Lesesaal EG

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  6. Article ; Online: To sleep perchance to dream…of pregnancy.

    Cromack, Sarah C / Walter, Jessica / Feinberg, Eve C

    Fertility and sterility

    2023  Volume 121, Issue 4, Page(s) 576–577

    MeSH term(s) Humans ; Pregnancy ; Female ; Sleep
    Language English
    Publishing date 2023-12-13
    Publishing country United States
    Document type Editorial
    ZDB-ID 80133-1
    ISSN 1556-5653 ; 0015-0282
    ISSN (online) 1556-5653
    ISSN 0015-0282
    DOI 10.1016/j.fertnstert.2023.12.010
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  7. Article ; Online: Supporting participants and study partners when trials end as planned.

    Walter, Sarah / Largent, Emily A / Edelmayer, Rebecca M

    Alzheimer's & dementia : the journal of the Alzheimer's Association

    2022  Volume 19, Issue 4, Page(s) 1590–1591

    Language English
    Publishing date 2022-11-28
    Publishing country United States
    Document type Letter
    ZDB-ID 2211627-8
    ISSN 1552-5279 ; 1552-5260
    ISSN (online) 1552-5279
    ISSN 1552-5260
    DOI 10.1002/alz.12872
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    In stock of ZB MED Cologne/Königswinter

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    Zs.MO 540: Show issues

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  8. Article ; Online: Achieving Diagnostic Excellence for Cancer: Symptom Detection as a Partner to Screening.

    Sarma, Elizabeth A / Walter, Fiona M / Kobrin, Sarah C

    JAMA

    2022  Volume 328, Issue 6, Page(s) 525–526

    MeSH term(s) Early Detection of Cancer/standards ; Humans ; Mass Screening/standards ; Neoplasms/diagnosis ; Research
    Language English
    Publishing date 2022-07-18
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2958-0
    ISSN 1538-3598 ; 0254-9077 ; 0002-9955 ; 0098-7484
    ISSN (online) 1538-3598
    ISSN 0254-9077 ; 0002-9955 ; 0098-7484
    DOI 10.1001/jama.2022.11744
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Reply on "Why compulsive sexual behavior is not a form of addiction like drug addiction".

    Stark, Rudolf / Walter, Bertram / Bengesser, Isabel / Kramer, Dietmar / Muhl, Christian / Tahmassebi, Nadja / Khatib, Said / Storz, Florian / Markert, Charlotte / Golder, Sarah

    Sexual medicine

    2024  Volume 12, Issue 1, Page(s) qfae007

    Language English
    Publishing date 2024-03-05
    Publishing country England
    Document type Journal Article
    ZDB-ID 2734882-9
    ISSN 2050-1161
    ISSN 2050-1161
    DOI 10.1093/sexmed/qfae007
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Modic changes in the lumbar vertebral column of chondrodystrophic and non-chondrodystrophic dogs with intervertebral disc disease.

    Agustini, Dyah / Heimann, Mary K / Co, Megan / Walter, Benjamin A / Purmessur, Devina / Moore, Sarah A

    Frontiers in veterinary science

    2024  Volume 11, Page(s) 1359016

    Abstract: Introduction: Modic changes (MC) are signs of vertebral pathology visible on magnetic resonance (MR) images that have been associated with low back pain (LBP) and disc degeneration in people. Multiple breeds of dogs also develop MCs and coincident back ... ...

    Abstract Introduction: Modic changes (MC) are signs of vertebral pathology visible on magnetic resonance (MR) images that have been associated with low back pain (LBP) and disc degeneration in people. Multiple breeds of dogs also develop MCs and coincident back pain. However, the association between breed, MC, and spinal pathologies has yet to be fully elucidated. This study aimed to identify the prevalence of MC that occur spontaneously in the lumbar vertebral column of dogs diagnosed with intervertebral disc disease (IVDD) and examine their association with demographic criteria and the disc width index (DWI).
    Methods: Medical records and lumbar vertebral column MR images were examined from 104 dogs (831 intervertebral disc spaces and adjacent vertebrae), which were divided into three groups: chondrodystrophic dogs (CD;
    Results: Increasing age and a diagnosis of IVDD were significantly associated with MC in dogs (
    Discussion: This study demonstrated that MC developed spontaneously in dogs, are common in dogs diagnosed with IVDD, and the type observed varies by breed. Further research is needed to understand the pathogenesis of MC; however, the increased presence of Type 2 MC in CD dogs, similar to what is found in people with disc degeneration, suggests that CD dogs could serve as models for MC in people.
    Language English
    Publishing date 2024-03-19
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2834243-4
    ISSN 2297-1769
    ISSN 2297-1769
    DOI 10.3389/fvets.2024.1359016
    Database MEDical Literature Analysis and Retrieval System OnLINE

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