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  1. Book: Systems biology of apoptosis

    Lavrik, Inna N.

    2013  

    Author's details Inna N. Lavrik
    Language English
    Size XII, 203 S. : Ill., graph. Darst.
    Publisher Springer
    Publishing place New York u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT017408104
    ISBN 978-1-4614-4008-6 ; 9781461440093 ; 1-4614-4008-4 ; 1461440092
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2012 A 3950 order for loan Magazin

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  2. Article: Editorial: Dynamical Networks of Life/Death Decisions in a Cell: From DNA Repair to Cell Death.

    Lavrik, Inna N

    Frontiers in cell and developmental biology

    2021  Volume 9, Page(s) 722426

    Language English
    Publishing date 2021-07-16
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2021.722426
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Modulation of extrinsic apoptotic pathway by intracellular glycosylation.

    Seyrek, Kamil / Ivanisenko, Nikita V / König, Corinna / Lavrik, Inna N

    Trends in cell biology

    2024  

    Abstract: ... by a single N-acetylglucosamine sugar is a dynamic and reversible PTM exhibiting properties more like ... phosphorylation than classical O- and N-linked glycosylation. Due to the sparse information existing, we have only ...

    Abstract The importance of post-translational modifications (PTMs), particularly O-GlcNAcylation, of cytoplasmic proteins in apoptosis has been neglected for quite a while. Modification of cytoplasmic proteins by a single N-acetylglucosamine sugar is a dynamic and reversible PTM exhibiting properties more like phosphorylation than classical O- and N-linked glycosylation. Due to the sparse information existing, we have only limited understanding of how GlcNAcylation affects cell death. Deciphering the role of GlcNAcylation in cell fate may provide further understanding of cell fate decisions. This review focus on the modulation of extrinsic apoptotic pathway via GlcNAcylation carried out by O-GlcNAc transferase (OGT) or by other bacterial effector proteins.
    Language English
    Publishing date 2024-02-08
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2024.01.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Editorial

    Inna N. Lavrik

    Frontiers in Cell and Developmental Biology, Vol

    Dynamical Networks of Life/Death Decisions in a Cell: From DNA Repair to Cell Death

    2021  Volume 9

    Keywords cell death ; DNA damage ; DNA repair ; mitophagy ; BER ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2021-07-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Book ; Online ; Thesis: Entschlüsselung neuer molekularer Mechanismen zur CD95/Fas-abhängigen Induktion des programmierten Zelltods

    Hillert-Richter, Laura Katharina Verfasser] / [Lavrik, Inna N. [Gutachter] / Brunner, Thomas [Gutachter]

    Entwicklung innovativer Ansätze zur gezielten Modifikation des CD95/Fas Signalweges

    2023  

    Author's details Laura Katharina Hillert-Richter ; Gutachter: Inna N. Lavrik, Thomas Brunner
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language German
    Publisher Universitätsbibliothek Otto-von-Guericke-Universität
    Publishing place Magdeburg
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  6. Article ; Online: The cross-talk of autophagy and apoptosis in breast carcinoma: implications for novel therapies?

    Seyrek, Kamil / Wohlfromm, Fabian / Espe, Johannes / Lavrik, Inna N

    The Biochemical journal

    2022  Volume 479, Issue 14, Page(s) 1581–1608

    Abstract: Breast cancer is still the most common cancer in women worldwide. Resistance to drugs and recurrence of the disease are two leading causes of failure in treatment. For a more efficient treatment of patients, the development of novel therapeutic regimes ... ...

    Abstract Breast cancer is still the most common cancer in women worldwide. Resistance to drugs and recurrence of the disease are two leading causes of failure in treatment. For a more efficient treatment of patients, the development of novel therapeutic regimes is needed. Recent studies indicate that modulation of autophagy in concert with apoptosis induction may provide a promising novel strategy in breast cancer treatment. Apoptosis and autophagy are two tightly regulated distinct cellular processes. To maintain tissue homeostasis abnormal cells are disposed largely by means of apoptosis. Autophagy, however, contributes to tissue homeostasis and cell fitness by scavenging of damaged organelles, lipids, proteins, and DNA. Defects in autophagy promote tumorigenesis, whereas upon tumor formation rapidly proliferating cancer cells may rely on autophagy to survive. Given that evasion of apoptosis is one of the characteristic hallmarks of cancer cells, inhibiting autophagy and promoting apoptosis can negatively influence cancer cell survival and increase cell death. Hence, combination of antiautophagic agents with the enhancement of apoptosis may restore apoptosis and provide a therapeutic advantage against breast cancer. In this review, we discuss the cross-talk of autophagy and apoptosis and the diverse facets of autophagy in breast cancer cells leading to novel models for more effective therapeutic strategies.
    MeSH term(s) Apoptosis ; Autophagy ; Breast Neoplasms/genetics ; Cell Line, Tumor ; Cell Survival ; Female ; Humans
    Language English
    Publishing date 2022-07-29
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20210676
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Measuring Composition of CD95 Death-Inducing Signaling Complex and Processing of Procaspase-8 in this Complex.

    Hillert-Richter, Laura K / Lavrik, Inna N

    Journal of visualized experiments : JoVE

    2021  , Issue 174

    Abstract: Extrinsic apoptosis is mediated by the activation of death receptors (DRs) such as CD95/Fas/APO-1 or tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-receptor 1/receptor 2 (TRAIL-R1/R2). Stimulation of these receptors with their cognate ... ...

    Abstract Extrinsic apoptosis is mediated by the activation of death receptors (DRs) such as CD95/Fas/APO-1 or tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-receptor 1/receptor 2 (TRAIL-R1/R2). Stimulation of these receptors with their cognate ligands leads to the assembly of the death-inducing signaling complex (DISC). DISC comprises DR, the adaptor protein Fas-associated protein with death domain (FADD), procaspases-8/-10, and cellular FADD-like interleukin (IL)-1β-converting enzyme-inhibitory proteins (c-FLIPs). The DISC serves as a platform for procaspase-8 processing and activation. The latter occurs via its dimerization/oligomerization in the death effector domain (DED) filaments assembled at the DISC. Activation of procaspase-8 is followed by its processing, which occurs in several steps. In this work, an established experimental workflow is described that allows the measurement of DISC formation and the processing of procaspase-8 in this complex. The workflow is based on immunoprecipitation techniques supported by western blot analysis. This workflow allows careful monitoring of different steps of procaspase-8 recruitment to the DISC and its processing and is highly relevant for investigating molecular mechanisms of extrinsic apoptosis.
    MeSH term(s) Apoptosis ; Caspase 8/metabolism ; Death Domain Receptor Signaling Adaptor Proteins/metabolism ; Signal Transduction ; fas Receptor/metabolism
    Chemical Substances Death Domain Receptor Signaling Adaptor Proteins ; fas Receptor ; Caspase 8 (EC 3.4.22.-)
    Language English
    Publishing date 2021-08-02
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Video-Audio Media
    ZDB-ID 2259946-0
    ISSN 1940-087X ; 1940-087X
    ISSN (online) 1940-087X
    ISSN 1940-087X
    DOI 10.3791/62842
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Modulation of CD95-mediated signaling by post-translational modifications: towards understanding CD95 signaling networks.

    Seyrek, Kamil / Lavrik, Inna N

    Apoptosis : an international journal on programmed cell death

    2019  Volume 24, Issue 5-6, Page(s) 385–394

    Abstract: CD95 is a member of the death receptor family and is well-known to promote apoptosis. However, accumulating evidence indicates that in some context CD95 has not only the potential to induce apoptosis but also can trigger non-apoptotic signal leading to ... ...

    Abstract CD95 is a member of the death receptor family and is well-known to promote apoptosis. However, accumulating evidence indicates that in some context CD95 has not only the potential to induce apoptosis but also can trigger non-apoptotic signal leading to cell survival, proliferation, cancer growth and metastasis. Despite extensive investigations focused on alterations in the expression level of CD95 and associated signal molecules, very few studies, however, have investigated the effects of post-translational modifications such as glycosylation, phosphorylation, palmitoylation, nitrosylation and glutathionylation on CD95 function. Post-translational modifications of CD95 in mammalian systems are likely to play a more prominent role than anticipated in CD95 induced cell death. In this review we will focus on the alterations in CD95-mediated signaling caused by post-translational modifications of CD95.
    MeSH term(s) Animals ; Apoptosis ; Caspases/metabolism ; Cell Survival ; Death Domain ; Fas Ligand Protein/metabolism ; Humans ; Protein Processing, Post-Translational/physiology ; Signal Transduction ; fas Receptor/chemistry ; fas Receptor/metabolism
    Chemical Substances Fas Ligand Protein ; fas Receptor ; Caspases (EC 3.4.22.-)
    Language English
    Publishing date 2019-05-08
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1452360-7
    ISSN 1573-675X ; 1360-8185
    ISSN (online) 1573-675X
    ISSN 1360-8185
    DOI 10.1007/s10495-019-01540-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 5178: Show issues Location:
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  9. Article ; Online: RL2 Enhances the Elimination of Breast Cancer Cells by Doxorubicin.

    Wohlfromm, Fabian / Seyrek, Kamil / Ivanisenko, Nikita / Troitskaya, Olga / Kulms, Dagmar / Richter, Vladimir / Koval, Olga / Lavrik, Inna N

    Cells

    2023  Volume 12, Issue 24

    Abstract: RL2 (recombinant lactaptin 2), a recombinant analogon of the human milk protein Κ-Casein, induces mitophagy and cell death in breast carcinoma cells. Furthermore, RL2 was shown to enhance extrinsic apoptosis upon long-term treatment while inhibiting it ... ...

    Abstract RL2 (recombinant lactaptin 2), a recombinant analogon of the human milk protein Κ-Casein, induces mitophagy and cell death in breast carcinoma cells. Furthermore, RL2 was shown to enhance extrinsic apoptosis upon long-term treatment while inhibiting it upon short-term stimulation. However, the effects of RL2 on the action of chemotherapeutic drugs that induce the intrinsic apoptotic pathway have not been investigated to date. Here, we examined the effects of RL2 on the doxorubicin (DXR)-induced cell death in breast cancer cells with three different backgrounds. In particular, we used BT549 and MDA-MB-231 triple-negative breast cancer (TNBC) cells, T47D estrogen receptor alpha (ERα) positive cells, and SKBR3 human epidermal growth factor receptor 2 (HER2) positive cells. BT549, MDA-MB-231, and T47D cells showed a severe loss of cell viability upon RL2 treatment, accompanied by the induction of mitophagy. Furthermore, BT549, MDA-MB-231, and T47D cells could be sensitized towards DXR treatment with RL2, as evidenced by loss of cell viability. In contrast, SKBR3 cells showed almost no RL2-induced loss of cell viability when treated with RL2 alone, and RL2 did not sensitize SKBR3 cells towards DXR-mediated loss of cell viability. Bioinformatic analysis of gene expression showed an enrichment of genes controlling metabolism in SKBR3 cells compared to the other cell lines. This suggests that the metabolic status of the cells is important for their sensitivity to RL2. Taken together, we have shown that RL2 can enhance the intrinsic apoptotic pathway in TNBC and ERα-positive breast cancer cells, paving the way for the development of novel therapeutic strategies.
    MeSH term(s) Humans ; Triple Negative Breast Neoplasms/drug therapy ; Estrogen Receptor alpha ; Cell Line, Tumor ; Apoptosis ; Doxorubicin/pharmacology
    Chemical Substances Estrogen Receptor alpha ; Doxorubicin (80168379AG)
    Language English
    Publishing date 2023-12-06
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells12242779
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Functional Role of N-Terminal Extension of Human AP Endonuclease 1 In Coordination of Base Excision DNA Repair via Protein-Protein Interactions.

    Moor, Nina / Vasil'eva, Inna / Lavrik, Olga

    International journal of molecular sciences

    2020  Volume 21, Issue 9

    Abstract: ... repair (BER) and other cellular processes. Its eukaryote-specific N-terminal extension plays diverse ... length and N-terminally truncated forms of APE1 (APE1NΔ35 and APE1NΔ61) for functionally and structurally ... Influence of the N-terminal truncation on binding the AP site-containing DNA was additionally explored ...

    Abstract Human apurinic/apyrimidinic endonuclease 1 (APE1) has multiple functions in base excision DNA repair (BER) and other cellular processes. Its eukaryote-specific N-terminal extension plays diverse regulatory roles in interaction with different partners. Here, we explored its involvement in interaction with canonical BER proteins. Using fluorescence based-techniques, we compared binding affinities of the full-length and N-terminally truncated forms of APE1 (APE1NΔ35 and APE1NΔ61) for functionally and structurally different DNA polymerase β (Polβ), X-ray repair cross-complementing protein 1 (XRCC1), and poly(adenosine diphosphate (ADP)-ribose) polymerase 1 (PARP1), in the absence and presence of model DNA intermediates. Influence of the N-terminal truncation on binding the AP site-containing DNA was additionally explored. These data suggest that the interaction domain for proteins is basically formed by the conserved catalytic core of APE1. The N-terminal extension being capable of dynamically interacting with the protein and DNA partners is mostly responsible for DNA-dependent modulation of protein-protein interactions. Polβ, XRCC1, and PARP1 were shown to more efficiently regulate the endonuclease activity of the full-length protein than that of APE1NΔ61, further suggesting contribution of the N-terminal extension to BER coordination. Our results advance the understanding of functional roles of eukaryote-specific protein extensions in highly coordinated BER processes.
    MeSH term(s) Binding Sites ; DNA/metabolism ; DNA Polymerase beta/metabolism ; DNA Repair ; DNA-(Apurinic or Apyrimidinic Site) Lyase/chemistry ; DNA-(Apurinic or Apyrimidinic Site) Lyase/genetics ; DNA-(Apurinic or Apyrimidinic Site) Lyase/metabolism ; Fluorescence ; Gene Expression Regulation ; Humans ; Mutation ; Poly (ADP-Ribose) Polymerase-1/metabolism ; Protein Binding ; Protein Domains ; Protein Interaction Maps ; X-ray Repair Cross Complementing Protein 1/metabolism
    Chemical Substances X-ray Repair Cross Complementing Protein 1 ; XRCC1 protein, human ; DNA (9007-49-2) ; PARP1 protein, human (EC 2.4.2.30) ; Poly (ADP-Ribose) Polymerase-1 (EC 2.4.2.30) ; DNA Polymerase beta (EC 2.7.7.7) ; POLB protein, human (EC 2.7.7.7) ; APEX1 protein, human (EC 4.2.99.18) ; DNA-(Apurinic or Apyrimidinic Site) Lyase (EC 4.2.99.18)
    Language English
    Publishing date 2020-04-28
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms21093122
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