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  1. Book: Endoplasmic reticulum stress in health and disease

    Agostinis, Patrizia / Samali, Afshin

    2012  

    Author's details Patrizia Agostinis ; Samali Afshin (ed.)
    Language English
    Size VIII, 452 S. : Ill., graph. Darst.
    Publisher Springer
    Publishing place Dordrecht u.a.
    Publishing country Netherlands
    Document type Book
    HBZ-ID HT017381353
    ISBN 978-94-007-4350-2 ; 9789400743519 ; 94-007-4350-5 ; 9400743513
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2012 A 3677 order for loan Magazin

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  2. Article ; Online: Unfolded protein response at the cross roads of tumourigenesis, oxygen sensing and drug resistance in clear cell renal cell carcinoma.

    Chee, Yew Hwang / Samali, Afshin / Robinson, Claire M

    Biochimica et biophysica acta. Reviews on cancer

    2022  Volume 1877, Issue 6, Page(s) 188814

    Abstract: Clear cell renal cell carcinoma (ccRCC) is the most common form of kidney cancer. Despite therapeutic advances, long term survival in patients diagnosed with advanced disease is low. Efforts to understand the mechanisms promoting disease progression will ...

    Abstract Clear cell renal cell carcinoma (ccRCC) is the most common form of kidney cancer. Despite therapeutic advances, long term survival in patients diagnosed with advanced disease is low. Efforts to understand the mechanisms promoting disease progression will likely produce novel therapeutic targets. The unfolded protein response (UPR) is activated when unfolded protein accumulates in the endoplasmic reticulum (ER) upon cellular stress. Constitutive UPR activation is a characteristic of many malignancies. We discuss the accumulating evidence that describes a role for the UPR in ccRCC. Studies focused on UPR signalling may provide compelling avenues for therapeutic intervention in the future.
    MeSH term(s) Humans ; Carcinoma, Renal Cell/drug therapy ; Carcinoma, Renal Cell/genetics ; Endoplasmic Reticulum Stress/physiology ; Oxygen ; Unfolded Protein Response ; Kidney Neoplasms/drug therapy ; Kidney Neoplasms/genetics ; Carcinogenesis ; Cell Transformation, Neoplastic ; Drug Resistance
    Chemical Substances Oxygen (S88TT14065)
    Language English
    Publishing date 2022-10-03
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 2918802-7
    ISSN 1879-2561 ; 0304-419X
    ISSN (online) 1879-2561
    ISSN 0304-419X
    DOI 10.1016/j.bbcan.2022.188814
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  3. Article ; Online: New insights into IRE1α activation and function in anti-tumor immunity.

    Logue, Susan E / Gorman, Adrienne M / Samali, Afshin

    The Journal of cell biology

    2022  Volume 221, Issue 6

    Abstract: Logue, Gorman, and Samali highlight a study by Guttman and colleagues (2022. J. Cell Biol.https://doi.org/10.1083/jcb.202111068) that shows exogenous antigen peptides imported into the ER can activate the ER stress sensor IRE1α, attenuating cross- ... ...

    Abstract Logue, Gorman, and Samali highlight a study by Guttman and colleagues (2022. J. Cell Biol.https://doi.org/10.1083/jcb.202111068) that shows exogenous antigen peptides imported into the ER can activate the ER stress sensor IRE1α, attenuating cross-presentation by dendritic cells.
    MeSH term(s) Antigen Presentation ; Dendritic Cells/immunology ; Endoplasmic Reticulum ; Endoplasmic Reticulum Stress ; Endoribonucleases/genetics ; Humans ; Neoplasms/immunology ; Peptides ; Protein Serine-Threonine Kinases/genetics
    Chemical Substances Peptides ; ERN1 protein, human (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Endoribonucleases (EC 3.1.-)
    Language English
    Publishing date 2022-05-11
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202205019
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Maintenance of Endoplasmic Reticulum Protein Homeostasis in Cancer: Friend or Foe.

    McMahon, Mari / Samali, Afshin / Chevet, Eric

    Progress in molecular and subcellular biology

    2021  Volume 59, Page(s) 197–214

    Abstract: The endoplasmic reticulum, as the site of synthesis for proteins in the secretory pathway has evolved select machineries to ensure the correct folding and modification of proteins. However, sometimes these quality control mechanisms fail and proteins are ...

    Abstract The endoplasmic reticulum, as the site of synthesis for proteins in the secretory pathway has evolved select machineries to ensure the correct folding and modification of proteins. However, sometimes these quality control mechanisms fail and proteins are misfolded. Other factors, such as nutrient deprivation, hypoxia or an increased demand on protein synthesis can also cause the accumulation of unfolded or misfolded proteins in the endoplasmic reticulum. There are mechanisms that recognise and deal with this accumulation of protein through degradation and/or export. Many diseases are associated with aberrant quality control mechanisms, and among these, cancer has emerged as a group of diseases that rely on endoplasmic reticulum homeostasis to sustain development and growth. The knowledge of how protein quality control operates in cancer has identified opportunities for these pathways to be pharmacologically targeted, which could lead to newer or more effective treatments in the future.
    MeSH term(s) Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum Stress/genetics ; Humans ; Neoplasms/genetics ; Neoplasms/metabolism ; Protein Folding ; Proteostasis/genetics
    Language English
    Publishing date 2021-05-29
    Publishing country United States
    Document type Journal Article
    ISSN 0079-6484
    ISSN 0079-6484
    DOI 10.1007/978-3-030-67696-4_10
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Correction: Dastghaib et al. Simvastatin Induces Unfolded Protein Response and Enhances Temozolomide-Induced Cell Death in Glioblastoma Cells.

    Dastghaib, Sanaz / Shojaei, Shahla / Mostafavi-Pour, Zohreh / Sharma, Pawan / Patterson, John B / Samali, Afshin / Mokarram, Pooneh / Ghavami, Saeid

    Cells

    2024  Volume 13, Issue 8

    Abstract: In the original publication [ ... ]. ...

    Abstract In the original publication [...].
    Language English
    Publishing date 2024-04-22
    Publishing country Switzerland
    Document type Published Erratum
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells13080722
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Insights into the structure and function of the RNA ligase RtcB.

    Moncan, Matthieu / Rakhsh-Khorshid, Hassan / Eriksson, Leif A / Samali, Afshin / Gorman, Adrienne M

    Cellular and molecular life sciences : CMLS

    2023  Volume 80, Issue 12, Page(s) 352

    Abstract: To be functional, some RNAs require a processing step involving splicing events. Each splicing event necessitates an RNA ligation step. RNA ligation is a process that can be achieved with various intermediaries such as self-catalysing RNAs, 5'-3' and 3'- ... ...

    Abstract To be functional, some RNAs require a processing step involving splicing events. Each splicing event necessitates an RNA ligation step. RNA ligation is a process that can be achieved with various intermediaries such as self-catalysing RNAs, 5'-3' and 3'-5' RNA ligases. While several types of RNA ligation mechanisms occur in human, RtcB is the only 3'-5' RNA ligase identified in human cells to date. RtcB RNA ligation activity is well known to be essential for the splicing of XBP1, an essential transcription factor of the unfolded protein response; as well as for the maturation of specific intron-containing tRNAs. As such, RtcB is a core factor in protein synthesis and homeostasis. Taking advantage of the high homology between RtcB orthologues in archaea, bacteria and eukaryotes, this review will provide an introduction to the structure of RtcB and the mechanism of 3'-5' RNA ligation. This analysis is followed by a description of the mechanisms regulating RtcB activity and localisation, its known partners and its various functions from bacteria to human with a specific focus on human cancer.
    MeSH term(s) Humans ; RNA Ligase (ATP)/genetics ; RNA Ligase (ATP)/chemistry ; RNA Ligase (ATP)/metabolism ; Transcription Factors/metabolism ; RNA/metabolism ; Unfolded Protein Response ; RNA, Transfer/genetics ; RNA, Transfer/metabolism ; RNA Splicing/genetics
    Chemical Substances RNA Ligase (ATP) (EC 6.5.1.3) ; Transcription Factors ; RNA (63231-63-0) ; RNA, Transfer (9014-25-9)
    Language English
    Publishing date 2023-11-07
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 1358415-7
    ISSN 1420-9071 ; 1420-682X
    ISSN (online) 1420-9071
    ISSN 1420-682X
    DOI 10.1007/s00018-023-05001-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 195: 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)

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  7. Article ; Online: Tumour Cell Secretome in Chemoresistance and Tumour Recurrence.

    Madden, Emma C / Gorman, Adrienne M / Logue, Susan E / Samali, Afshin

    Trends in cancer

    2020  Volume 6, Issue 6, Page(s) 489–505

    Abstract: Chemoresistance is a major factor driving tumour relapse and the high rates of cancer-related deaths. Understanding how cancer cells overcome chemotherapy-induced cell death is critical in promoting patient survival. One emerging mechanism of ... ...

    Abstract Chemoresistance is a major factor driving tumour relapse and the high rates of cancer-related deaths. Understanding how cancer cells overcome chemotherapy-induced cell death is critical in promoting patient survival. One emerging mechanism of chemoresistance is the tumour cell secretome (TCS), an array of protumorigenic factors released by tumour cells. Chemotherapy exposure can also alter the composition of the TCS, known as therapy-induced TCS, and can promote tumour relapse and the formation of an immunosuppressive tumour microenvironment (TME). Here, we outline how the TCS can protect cancer cells from chemotherapy-induced cell death. We also highlight recent evidence describing how therapy-induced TCS can impact cancer stem cell (CSC) expansion and tumour-associated immune cells to enable tumour regrowth and antitumour immunity.
    MeSH term(s) Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Apoptosis/drug effects ; Apoptosis/immunology ; Cell Line, Tumor ; Cell Survival/drug effects ; Cell Survival/immunology ; Drug Resistance, Neoplasm/drug effects ; Drug Resistance, Neoplasm/immunology ; Humans ; Neoplasm Recurrence, Local/immunology ; Neoplasm Recurrence, Local/pathology ; Neoplasm Recurrence, Local/prevention & control ; Neoplasms/drug therapy ; Neoplasms/immunology ; Neoplasms/pathology ; Neoplastic Stem Cells/drug effects ; Neoplastic Stem Cells/immunology ; Neoplastic Stem Cells/pathology ; Tumor Escape/drug effects ; Tumor Escape/immunology ; Tumor Microenvironment/drug effects ; Tumor Microenvironment/immunology
    Chemical Substances Antineoplastic Agents
    Language English
    Publishing date 2020-03-25
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2852626-0
    ISSN 2405-8025 ; 2405-8033 ; 2405-8033
    ISSN (online) 2405-8025 ; 2405-8033
    ISSN 2405-8033
    DOI 10.1016/j.trecan.2020.02.020
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: An Emerging Role for the Unfolded Protein Response in Pancreatic Cancer.

    Robinson, Claire M / Talty, Aaron / Logue, Susan E / Mnich, Katarzyna / Gorman, Adrienne M / Samali, Afshin

    Cancers

    2021  Volume 13, Issue 2

    Abstract: Pancreatic ductal adenocarcinoma (PDAC) is the most common form of pancreatic cancer and one of the leading causes of cancer-associated deaths in the world. It is characterised by dismal response rates to conventional therapies. A major challenge in ... ...

    Abstract Pancreatic ductal adenocarcinoma (PDAC) is the most common form of pancreatic cancer and one of the leading causes of cancer-associated deaths in the world. It is characterised by dismal response rates to conventional therapies. A major challenge in treatment strategies for PDAC is the presence of a dense stroma that surrounds the tumour cells, shielding them from treatment. This unique tumour microenvironment is fuelled by paracrine signalling between pancreatic cancer cells and supporting stromal cell types including the pancreatic stellate cells (PSC). While our molecular understanding of PDAC is improving, there remains a vital need to develop effective, targeted treatments. The unfolded protein response (UPR) is an elaborate signalling network that governs the cellular response to perturbed protein homeostasis in the endoplasmic reticulum (ER) lumen. There is growing evidence that the UPR is constitutively active in PDAC and may contribute to the disease progression and the acquisition of resistance to therapy. Given the importance of the tumour microenvironment and cytokine signalling in PDAC, and an emerging role for the UPR in shaping the tumour microenvironment and in the regulation of cytokines in other cancer types, this review explores the importance of the UPR in PDAC biology and its potential as a therapeutic target in this disease.
    Language English
    Publishing date 2021-01-12
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2527080-1
    ISSN 2072-6694
    ISSN 2072-6694
    DOI 10.3390/cancers13020261
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Regulation of lipid metabolism by the unfolded protein response.

    Moncan, Matthieu / Mnich, Katarzyna / Blomme, Arnaud / Almanza, Aitor / Samali, Afshin / Gorman, Adrienne M

    Journal of cellular and molecular medicine

    2021  Volume 25, Issue 3, Page(s) 1359–1370

    Abstract: The endoplasmic reticulum (ER) is the site of protein folding and secretion, ... ...

    Abstract The endoplasmic reticulum (ER) is the site of protein folding and secretion, Ca
    MeSH term(s) Animals ; Biomarkers ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum Stress ; Gene Expression Regulation ; Humans ; Lipid Metabolism ; Metabolic Networks and Pathways ; Unfolded Protein Response
    Chemical Substances Biomarkers
    Language English
    Publishing date 2021-01-04
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2074559-X
    ISSN 1582-4934 ; 1582-4934 ; 1582-1838
    ISSN (online) 1582-4934
    ISSN 1582-4934 ; 1582-1838
    DOI 10.1111/jcmm.16255
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5752: Show issues Location:
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  10. Book: Endoplasmic reticulum stress in health and disease

    Agostinis, Patrizia / Samali, Afshin

    2012  

    Author's details Patrizia Agostinis, Afshin Samali, (eds)
    MeSH term(s) Endoplasmic Reticulum Stress
    Language English
    Size viii, 452 p. :, ill. (some col.) ;, 24 cm.
    Publisher Springer
    Publishing place Dordrecht
    Document type Book
    ISBN 9789400743502 ; 9400743505 ; 9789400743519 ; 9400743513
    Database Catalogue of the US National Library of Medicine (NLM)

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