LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 622

Search options

  1. Book ; Online ; E-Book: Ras

    O'Bryan, John P. / Piazza, Gary A.

    past, present, and future

    (Advances in cancer research ; Volume 153)

    2022  

    Author's details edited by John P. O'Bryan, Gary A. Piazza
    Series title Advances in cancer research ; Volume 153
    Keywords Ras oncogenes
    Subject code 616.994071
    Language English
    Size 1 online resource (358 pages)
    Publisher Academic Press
    Publishing place Cambridge, Massachusetts
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    ISBN 0-12-824486-0 ; 9780128244852 ; 978-0-12-824486-9 ; 0128244852
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

    Full text online

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  2. Article ; Online: Probing RAS Function Using Monobody and NanoBiT Technologies.

    Whaby, Michael / Nair, Rakesh Sathish / O'Bryan, John P

    Methods in molecular biology (Clifton, N.J.)

    2024  Volume 2797, Page(s) 211–225

    Abstract: Missense mutations in the RAS family of oncogenes (HRAS, KRAS, and NRAS) are present in approximately 20% of human cancers, making RAS a valuable therapeutic target (Prior et al., Cancer Res 80:2969-2974, 2020). Although decades of research efforts to ... ...

    Abstract Missense mutations in the RAS family of oncogenes (HRAS, KRAS, and NRAS) are present in approximately 20% of human cancers, making RAS a valuable therapeutic target (Prior et al., Cancer Res 80:2969-2974, 2020). Although decades of research efforts to develop therapeutic inhibitors of RAS were unsuccessful, there has been success in recent years with the entrance of FDA-approved KRAS
    MeSH term(s) Humans ; Proto-Oncogene Proteins p21(ras) ; Neoplasms/drug therapy ; Neoplasms/genetics ; Oncogenes ; Cell Communication ; Mutation ; Luciferases
    Chemical Substances nanoluc (EC 1.13.12.-) ; Proto-Oncogene Proteins p21(ras) (EC 3.6.5.2) ; Luciferases (EC 1.13.12.-)
    Language English
    Publishing date 2024-04-03
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3822-4_15
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  3. Article ; Online: Intersectin - many facets of a scaffold protein.

    Mintoo, Mubashir / Rajagopalan, Vinodh / O'Bryan, John P

    Biochemical Society transactions

    2024  Volume 52, Issue 1, Page(s) 1–13

    Abstract: Intersectin (ITSN) is a multi-domain scaffold protein with a diverse array of functions including regulation of endocytosis, vesicle transport, and activation of various signal transduction pathways. There are two ITSN genes located on chromosomes 21 and ...

    Abstract Intersectin (ITSN) is a multi-domain scaffold protein with a diverse array of functions including regulation of endocytosis, vesicle transport, and activation of various signal transduction pathways. There are two ITSN genes located on chromosomes 21 and 2 encoding for proteins ITSN1 and ITSN2, respectively. Each ITSN gene encodes two major isoforms, ITSN-Long (ITSN-L) and ITSN-Short (ITSN-S), due to alternative splicing. ITSN1 and 2, collectively referred to as ITSN, are implicated in many physiological and pathological processes, such as neuronal maintenance, actin cytoskeletal rearrangement, and tumor progression. ITSN is mis-regulated in many tumors, such as breast, lung, neuroblastomas, and gliomas. Altered expression of ITSN is also found in several neurodegenerative diseases, such as Down Syndrome and Alzheimer's disease. This review summarizes recent studies on ITSN and provides an overview of the function of this important family of scaffold proteins in various biological processes.
    MeSH term(s) Humans ; Signal Transduction ; Adaptor Proteins, Vesicular Transport/genetics ; Adaptor Proteins, Vesicular Transport/metabolism ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Down Syndrome/genetics ; Down Syndrome/metabolism ; Down Syndrome/pathology ; Endocytosis/physiology
    Chemical Substances intersectin 1 ; Adaptor Proteins, Vesicular Transport ; Protein Isoforms
    Language English
    Publishing date 2024-02-27
    Publishing country England
    Document type Review ; Journal Article
    ZDB-ID 184237-7
    ISSN 1470-8752 ; 0300-5127
    ISSN (online) 1470-8752
    ISSN 0300-5127
    DOI 10.1042/BST20211241
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 944: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: Preface.

    O'Bryan, John P / Piazza, Gary A

    Advances in cancer research

    2021  Volume 153, Page(s) xiii–xiv

    Language English
    Publishing date 2021-08-20
    Publishing country United States
    Document type Editorial
    ZDB-ID 127-2
    ISSN 2162-5557 ; 0065-230X
    ISSN (online) 2162-5557
    ISSN 0065-230X
    DOI 10.1016/S0065-230X(22)00012-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uh III Zs.178: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article ; Online: Pharmacological targeting of RAS: Recent success with direct inhibitors.

    O'Bryan, John P

    Pharmacological research

    2018  Volume 139, Page(s) 503–511

    Abstract: RAS has long been viewed as undruggable due to its lack of deep pockets for binding of small molecule inhibitors. However, recent successes in the development of direct RAS inhibitors suggest that the goal of pharmacological inhibition of RAS in patients ...

    Abstract RAS has long been viewed as undruggable due to its lack of deep pockets for binding of small molecule inhibitors. However, recent successes in the development of direct RAS inhibitors suggest that the goal of pharmacological inhibition of RAS in patients may soon be realized. This review will discuss the role of RAS in cancer, the approaches used to develop direct RAS inhibitors, and highlight recent successes in the development of novel RAS inhibitory compounds that target different aspects of RAS biochemistry. In particular, this review will discuss the different properties of RAS that have been targeted by various inhibitors including membrane localization, the different activation states of RAS, effector binding, and nucleotide exchange. In addition, this review will highlight the recent success with mutation-specific inhibitors that exploit the unique biochemistry of the RAS(G12C) mutant. Although this mutation in KRAS accounts for 11% of all KRAS mutations in cancer, it is the most prominent KRAS mutant in lung cancer suggesting that G12C-specific inhibitors may provide a new approach for treating the subset of lung cancer patients harboring this mutant allele. Finally, this review will discuss the involvement of dimerization in RAS function and highlight new approaches to inhibit RAS by specifically interfering with RAS:RAS interaction.
    MeSH term(s) Animals ; Antineoplastic Agents/therapeutic use ; Cell Membrane/metabolism ; Humans ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Protein Multimerization ; ras Proteins/antagonists & inhibitors ; ras Proteins/chemistry ; ras Proteins/metabolism
    Chemical Substances Antineoplastic Agents ; ras Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2018-10-23
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 1003347-6
    ISSN 1096-1186 ; 0031-6989 ; 1043-6618
    ISSN (online) 1096-1186
    ISSN 0031-6989 ; 1043-6618
    DOI 10.1016/j.phrs.2018.10.021
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 721: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article: PAs and NPs in employee health during the COVID-19 pandemic.

    O'Bryan, Pauline / Cutrell, James / Gonzalez, John D / Namiranian, Azadeh

    JAAPA : official journal of the American Academy of Physician Assistants

    2023  Volume 36, Issue 3, Page(s) 42–45

    Abstract: Abstract: COVID-19 created unprecedented occupational health challenges for hospitals. To meet these demands at a large county safety-net hospital, a COVID-19 employee response team led by PAs and NPs was created. From April 2020 through February 2022, ... ...

    Abstract Abstract: COVID-19 created unprecedented occupational health challenges for hospitals. To meet these demands at a large county safety-net hospital, a COVID-19 employee response team led by PAs and NPs was created. From April 2020 through February 2022, this team managed more than 14,000 discrete employee contacts related to COVID-19 employee concerns. This article describes our experience in creating this team and highlights key strengths and lessons for other institutions seeking to adopt similar models.
    MeSH term(s) Humans ; COVID-19 ; Occupational Health ; Pandemics
    Language English
    Publishing date 2023-01-30
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2415226-2
    ISSN 0893-7400 ; 1547-1896
    ISSN (online) 0893-7400
    ISSN 1547-1896
    DOI 10.1097/01.JAA.0000918760.24764.71
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 6624: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article ; Online: Targeting the "undruggable" RAS with biologics.

    Whaby, Michael / Khan, Imran / O'Bryan, John P

    Advances in cancer research

    2021  Volume 153, Page(s) 237–266

    Abstract: RAS proteins represent critical drivers of tumor development and thus are the focus of intense efforts to pharmacologically inhibit these proteins in human cancer. Although recent success has been attained in developing clinically efficacious inhibitors ... ...

    Abstract RAS proteins represent critical drivers of tumor development and thus are the focus of intense efforts to pharmacologically inhibit these proteins in human cancer. Although recent success has been attained in developing clinically efficacious inhibitors to KRAS
    MeSH term(s) Biological Products/pharmacology ; Biological Products/therapeutic use ; Humans ; Mutation ; Neoplasms/pathology ; ras Proteins/metabolism
    Chemical Substances Biological Products ; ras Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2021-08-13
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 127-2
    ISSN 2162-5557 ; 0065-230X
    ISSN (online) 2162-5557
    ISSN 0065-230X
    DOI 10.1016/bs.acr.2021.07.006
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uh III Zs.178: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  8. Article ; Online: Probing RAS Function with Monobodies.

    Khan, Imran / O'Bryan, John P

    Methods in molecular biology (Clifton, N.J.)

    2021  Volume 2262, Page(s) 281–302

    Abstract: RAS is frequently mutated in human cancers with nearly 20% of all cancers harboring mutations in one of three RAS isoforms (KRAS, HRAS, or NRAS). Furthermore, RAS proteins are critical oncogenic drivers of tumorigenesis. As such, RAS has been a prime ... ...

    Abstract RAS is frequently mutated in human cancers with nearly 20% of all cancers harboring mutations in one of three RAS isoforms (KRAS, HRAS, or NRAS). Furthermore, RAS proteins are critical oncogenic drivers of tumorigenesis. As such, RAS has been a prime focus for development of targeted cancer therapeutics. Although RAS is viewed by many as undruggable, the recent development of allele-specific covalent inhibitors to KRAS(G12C) has provided significant hope for the eventual pharmacological inhibition of RAS (Ostrem et al., Nature 503(7477):548-551, 2013; Patricelli et al., Cancer Discov 6(3):316-329, 2016; Janes et al., Cell 172(3):578-589.e17, 2018; Canon et al., Nature 575(7781):217-223, 2019; Hallin et al., Cancer Discov 10(1):54-71, 2020). Indeed, these (G12C)-specific inhibitors have elicited promising responses in early phase clinical trials (Canon et al., Nature 575(7781):217-223, 2019; Hallin et al., Cancer Discov 10(1):54-71, 2020). Despite this success in pharmacologically targeting KRAS(G12C), the remaining RAS mutants lack readily tractable chemistries for development of covalent inhibitors. Thus, alternative approaches are needed to develop broadly efficacious RAS inhibitors. We have utilized Monobody (Mb) technology to identify vulnerabilities in RAS that can potentially be exploited for development of novel RAS inhibitors. Here, we describe the methods used to isolate RAS-specific Mbs and to define their inhibitory activity.
    MeSH term(s) Antineoplastic Agents/pharmacology ; Humans ; Molecular Targeted Therapy/methods ; Neoplasms/drug therapy ; Neoplasms/immunology ; Neoplasms/metabolism ; Neoplasms/pathology ; Protein Engineering/methods ; Single-Domain Antibodies/immunology ; ras Proteins/antagonists & inhibitors ; ras Proteins/immunology
    Chemical Substances Antineoplastic Agents ; Single-Domain Antibodies ; ras Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2021-05-12
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-1190-6_17
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  9. Article ; Online: Biology, pathology, and therapeutic targeting of RAS.

    Rhett, J Matthew / Khan, Imran / O'Bryan, John P

    Advances in cancer research

    2020  Volume 148, Page(s) 69–146

    Abstract: RAS was identified as a human oncogene in the early 1980s and subsequently found to be mutated in nearly 30% of all human cancers. More importantly, RAS plays a central role in driving tumor development and maintenance. Despite decades of effort, there ... ...

    Abstract RAS was identified as a human oncogene in the early 1980s and subsequently found to be mutated in nearly 30% of all human cancers. More importantly, RAS plays a central role in driving tumor development and maintenance. Despite decades of effort, there remain no FDA approved drugs that directly inhibit RAS. The prevalence of RAS mutations in cancer and the lack of effective anti-RAS therapies stem from RAS' core role in growth factor signaling, unique structural features, and biochemistry. However, recent advances have brought promising new drugs to clinical trials and shone a ray of hope in the field. Here, we will exposit the details of RAS biology that illustrate its key role in cell signaling and shed light on the difficulties in therapeutically targeting RAS. Furthermore, past and current efforts to develop RAS inhibitors will be discussed in depth.
    MeSH term(s) Animals ; Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Humans ; Molecular Targeted Therapy ; Mutation ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Neoplasms/pathology ; Oncogenes ; Signal Transduction/physiology ; ras Proteins/antagonists & inhibitors ; ras Proteins/genetics ; ras Proteins/metabolism
    Chemical Substances Antineoplastic Agents ; ras Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2020-07-09
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 127-2
    ISSN 2162-5557 ; 0065-230X
    ISSN (online) 2162-5557
    ISSN 0065-230X
    DOI 10.1016/bs.acr.2020.05.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uh III Zs.178: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  10. Article ; Online: Inhibition of RAS: proven and potential vulnerabilities.

    Zuberi, Mariyam / Khan, Imran / O'Bryan, John P

    Biochemical Society transactions

    2020  Volume 48, Issue 5, Page(s) 1831–1841

    Abstract: RAS is a membrane localized small GTPase frequently mutated in human cancer. As such, RAS has been a focal target for developing cancer therapeutics since its discovery nearly four decades ago. However, efforts to directly target RAS have been ... ...

    Abstract RAS is a membrane localized small GTPase frequently mutated in human cancer. As such, RAS has been a focal target for developing cancer therapeutics since its discovery nearly four decades ago. However, efforts to directly target RAS have been challenging due to the apparent lack of readily discernable deep pockets for binding small molecule inhibitors leading many to consider RAS as undruggable. An important milestone in direct RAS inhibition was achieved recently with the groundbreaking discovery of covalent inhibitors that target the mutant Cys residue in KRAS(G12C). Surprisingly, these G12C-reactive compounds only target mutant RAS in the GDP-bound state thereby locking it in the inactive conformation and blocking its ability to couple with downstream effector pathways. Building on this success, several groups have developed similar compounds that selectively target KRAS(G12C), with AMG510 and MRTX849 the first to advance to clinical trials. Both have shown early promising results. Though the success with these compounds has reignited the possibility of direct pharmacological inhibition of RAS, these covalent inhibitors are limited to treating KRAS(G12C) tumors which account for <15% of all RAS mutants in human tumors. Thus, there remains an unmet need to identify more broadly efficacious RAS inhibitors. Here, we will discuss the current state of RAS(G12C) inhibitors and the potential for inhibiting additional RAS mutants through targeting RAS dimerization which has emerged as an important step in the allosteric regulation of RAS function.
    MeSH term(s) Acetonitriles/pharmacology ; Allosteric Regulation ; Allosteric Site ; Animals ; Antineoplastic Agents/pharmacology ; Catalytic Domain ; Cell Membrane/metabolism ; Dimerization ; Drug Design ; GTP Phosphohydrolases/metabolism ; Humans ; Metabolism ; Mice ; Molecular Conformation ; Mutation ; Neoplasm Transplantation ; Neoplasms/metabolism ; Neoplasms/therapy ; Piperazines/pharmacology ; Protein Conformation ; Proto-Oncogene Proteins p21(ras)/antagonists & inhibitors ; Pyridines/pharmacology ; Pyridines/therapeutic use ; Pyrimidines/pharmacology ; Pyrimidines/therapeutic use ; Signal Transduction/drug effects ; ras Proteins/antagonists & inhibitors ; ras Proteins/metabolism
    Chemical Substances Acetonitriles ; Antineoplastic Agents ; KRAS protein, human ; Piperazines ; Pyridines ; Pyrimidines ; sotorasib (2B2VM6UC8G) ; adagrasib (8EOO6HQF8Y) ; GTP Phosphohydrolases (EC 3.6.1.-) ; Proto-Oncogene Proteins p21(ras) (EC 3.6.5.2) ; ras Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2020-09-01
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 184237-7
    ISSN 1470-8752 ; 0300-5127
    ISSN (online) 1470-8752
    ISSN 0300-5127
    DOI 10.1042/BST20190023
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 944: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top