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  1. Article ; Online: Overexpression of Endoplasmic Reticulum Proteins from Arabidopsis thaliana in Baculovirus.

    Bolanos-Garcia, Victor M

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

    2024  Volume 2772, Page(s) 311–322

    Abstract: The overproduction of proteins of the endoplasmic reticulum (ER) of plant cells in prokaryotic heterologous gene expression system remains a technical challenge. Recent advances in genetically modified insect cell technology and virus engineering methods ...

    Abstract The overproduction of proteins of the endoplasmic reticulum (ER) of plant cells in prokaryotic heterologous gene expression system remains a technical challenge. Recent advances in genetically modified insect cell technology and virus engineering methods have paved the way to produce recombinant ER plant proteins, including those harboring posttranslational modifications, and therefore, to yield ER plant proteins that are natively folded and fully functional. The present contribution focuses on the baculovirus-expression system flashBAC, which overcomes certain technical hurdles found in other insect cell-based expression systems such as the generation of a bacmid and the negative selection of recombinant clones.
    MeSH term(s) Arabidopsis/genetics ; Baculoviridae/genetics ; Plant Proteins ; Clone Cells ; Endoplasmic Reticulum
    Chemical Substances Plant Proteins
    Language English
    Publishing date 2024-02-27
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3710-4_24
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: On the Regulation of Mitosis by the Kinetochore, a Macromolecular Complex and Organising Hub of Eukaryotic Organisms.

    Bolanos-Garcia, Victor M

    Sub-cellular biochemistry

    2022  Volume 99, Page(s) 235–267

    Abstract: The kinetochore is the multiprotein complex of eukaryotic organisms that is assembled on mitotic or meiotic centromeres to connect centromeric DNA with microtubules. Its function involves the coordinated action of more than 100 different proteins. The ... ...

    Abstract The kinetochore is the multiprotein complex of eukaryotic organisms that is assembled on mitotic or meiotic centromeres to connect centromeric DNA with microtubules. Its function involves the coordinated action of more than 100 different proteins. The kinetochore acts as an organiser hub that establishes physical connections with microtubules and centromere-associated proteins and recruits central protein components of the spindle assembly checkpoint (SAC), an evolutionarily conserved surveillance mechanism of eukaryotic organisms that detects unattached kinetochores and destabilises incorrect kinetochore-microtubule attachments. The molecular communication between the kinetochore and the SAC is highly dynamic and tightly regulated to ensure that cells can progress towards anaphase until each chromosome is properly bi-oriented on the mitotic spindle. This is achieved through an interplay of highly cooperative interactions and concerted phosphorylation/dephosphorylation events that are organised in time and space.This contribution discusses our current understanding of the function, structure and regulation of the kinetochore, in particular, how its communication with the SAC results in the amplification of specific signals to exquisitely control the eukaryotic cell cycle. This contribution also addresses recent advances in machine learning approaches, cell imaging and proteomics techniques that have enhanced our understanding of the molecular mechanisms that ensure the high fidelity and timely segregation of the genetic material every time a cell divides as well as the current challenges in the study of this fascinating molecular machine.
    MeSH term(s) Chromosome Segregation ; Eukaryota/genetics ; Kinetochores ; Microtubules/metabolism ; Mitosis ; Spindle Apparatus/metabolism
    Language English
    Publishing date 2022-09-23
    Publishing country United States
    Document type Journal Article
    ISSN 0306-0225 ; 0096-8757
    ISSN 0306-0225 ; 0096-8757
    DOI 10.1007/978-3-031-00793-4_7
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  3. Article: The spindle checkpoint proteins BUB1 and BUBR1: (SLiM)ming down to the basics.

    Elowe, Sabine / Bolanos-Garcia, Victor M

    Trends in biochemical sciences

    2022  Volume 47, Issue 4, Page(s) 352–366

    Abstract: Benzimidazole 1 (BUB1) and budding uninhibited by benzimidazole 1-related 1 (BUBR1) are multidomain paralogs with key roles in chromosome alignment during mitosis and the spindle assembly checkpoint (SAC), an evolutionarily conserved signaling pathway ... ...

    Abstract Benzimidazole 1 (BUB1) and budding uninhibited by benzimidazole 1-related 1 (BUBR1) are multidomain paralogs with key roles in chromosome alignment during mitosis and the spindle assembly checkpoint (SAC), an evolutionarily conserved signaling pathway that monitors errors in chromosome segregation during cell division in eukaryotes. Although BUB1 and BUBR1 share a similar domain organization and short linear interaction motifs (SLiMs), they control distinct aspects of chromosome congression and the SAC. Here we discuss the roles of BUB1 and BUBR1 SLiMs in mitosis and complement this with additional insights gleamed from studying their evolution. We show that BUB1 and BUBR1 SLiMs form highly specific interactions that are carefully orchestrated in space and time and contend that they define BUB1 and BUBR1 as organizing hubs that drive SAC signaling and ensure genome stability.
    MeSH term(s) Cell Cycle Proteins/metabolism ; Chromosome Segregation ; Kinetochores/metabolism ; Mitosis ; Protein Serine-Threonine Kinases ; Signal Transduction ; Spindle Apparatus/metabolism
    Chemical Substances Cell Cycle Proteins ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2022-02-17
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; 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.2022.01.004
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1207: 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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  4. Article: Protein Complexes in the Nucleus: The Control of Chromosome Segregation.

    Bolanos-Garcia, Victor M

    Sub-cellular biochemistry

    2017  Volume 83, Page(s) 455–481

    Abstract: Mistakes in the process of cell division can lead to the loss, gain or rearrangement of chromosomes. Significant chromosomal abnormalities are usually lethal to the cells and cause spontaneous miscarriages. However, in some cases, defects in the spindle ... ...

    Abstract Mistakes in the process of cell division can lead to the loss, gain or rearrangement of chromosomes. Significant chromosomal abnormalities are usually lethal to the cells and cause spontaneous miscarriages. However, in some cases, defects in the spindle assembly checkpoint lead to severe diseases, such as cancer and birth and development defects, including Down's syndrome. The timely and accurate control of chromosome segregation in mitosis relies on the spindle assembly checkpoint (SAC), an evolutionary conserved, self-regulated signalling system present in higher organisms. The spindle assembly checkpoint is orchestrated by dynamic interactions between spindle microtubules and the kinetochore , a multiprotein complex that constitutes the site for attachment of chromosomes to microtubule polymers to pull sister chromatids apart during cell division. This chapter discusses the current molecular understanding of the essential, highly dynamic molecular interactions underpinning spindle assembly checkpoint signalling and how the complex choreography of interactions can be coordinated in time and space to finely regulate the process. The potential of targeting this signalling pathway to interfere with the abnormal segregation of chromosomes, which occurs in diverse malignancies and the new opportunities that recent technological developments are opening up for a deeper understanding of the spindle assembly checkpoint are also discussed.
    MeSH term(s) Cell Cycle Proteins/metabolism ; Cell Nucleus/chemistry ; Cell Nucleus/metabolism ; Chromosome Segregation ; Humans ; Kinetochores/chemistry ; Kinetochores/metabolism ; Microtubules/chemistry ; Microtubules/metabolism ; Mitosis ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/metabolism ; Spindle Apparatus/chemistry ; Spindle Apparatus/metabolism
    Chemical Substances Cell Cycle Proteins ; Multiprotein Complexes
    Language English
    Publishing date 2017-03-07
    Publishing country United States
    Document type Journal Article
    ISSN 0306-0225 ; 0096-8757
    ISSN 0306-0225 ; 0096-8757
    DOI 10.1007/978-3-319-46503-6_16
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  5. Article: Editorial: E3 ubiquitin ligases: From structure to physiology to therapeutics, Volume II.

    Licchesi, Julien D F / Laman, Heike / Ikeda, Fumiyo / Ferguson, Fleur M / Bolanos-Garcia, Victor M

    Frontiers in physiology

    2022  Volume 13, Page(s) 1038793

    Language English
    Publishing date 2022-09-27
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2564217-0
    ISSN 1664-042X
    ISSN 1664-042X
    DOI 10.3389/fphys.2022.1038793
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  6. Article ; Online: The

    Rabanal, Francesc / Johnson, Mark S / Alaimo, Alessandro / Bolanos-Garcia, Victor M / Beddoe, Travis

    Biomolecules

    2022  Volume 12, Issue 1

    Abstract: We are glad to share with you our first Journal Club and to highlight some of the most interesting papers published recently [ ... ]. ...

    Abstract We are glad to share with you our first Journal Club and to highlight some of the most interesting papers published recently [...].
    MeSH term(s) Animals ; Anti-Bacterial Agents ; Humans ; Periodicals as Topic
    Chemical Substances Anti-Bacterial Agents
    Language English
    Publishing date 2022-01-06
    Publishing country Switzerland
    Document type Editorial ; Research Support, Non-U.S. Gov't
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom12010086
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  7. Article: The Anaphase Promoting Complex/Cyclosome (APC/C): A Versatile E3 Ubiquitin Ligase.

    Curtis, Natalie L / Bolanos-Garcia, Victor M

    Sub-cellular biochemistry

    2020  Volume 93, Page(s) 539–623

    Abstract: In the present chapter we discuss the essential roles of the human E3 ubiquitin ligase Anaphase Promoting Complex/Cyclosome (APC/C) in mitosis as well as the emerging evidence of important APC/C roles in cellular processes beyond cell division control ... ...

    Abstract In the present chapter we discuss the essential roles of the human E3 ubiquitin ligase Anaphase Promoting Complex/Cyclosome (APC/C) in mitosis as well as the emerging evidence of important APC/C roles in cellular processes beyond cell division control such as regulation of genomic integrity and cell differentiation of the nervous system. We consider the potential incipient role of APC/C dysregulation in the pathophysiology of the neurological disorder Alzheimer's disease (AD). We also discuss how certain Deoxyribonucleic Acid (DNA) and Ribonucleic Acid (RNA) viruses take control of the host's cell division regulatory system through harnessing APC/C ubiquitin ligase activity and hypothesise the plausible molecular mechanisms underpinning virus manipulation of the APC/C. We also examine how defects in the function of this multisubunit protein assembly drive abnormal cell proliferation and lastly argue the potential of APC/C as a promising therapeutic target for the development of innovative therapies for the treatment of chronic malignancies such as cancer.
    MeSH term(s) Anaphase-Promoting Complex-Cyclosome/antagonists & inhibitors ; Anaphase-Promoting Complex-Cyclosome/metabolism ; Humans ; Mitosis ; Neoplasms/drug therapy ; Neoplasms/enzymology ; Neoplasms/pathology ; Ubiquitination
    Chemical Substances Anaphase-Promoting Complex-Cyclosome (EC 2.3.2.27)
    Language English
    Publishing date 2020-01-14
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 0306-0225 ; 0096-8757
    ISSN 0306-0225 ; 0096-8757
    DOI 10.1007/978-3-030-28151-9_18
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  8. Article: Biochemical, biophysical, and functional characterisation of the E3 ubiquitin ligase APC/C regulator CDC20 from

    Cosma, Maria-Alexa / Curtis, Natalie L / Pain, Charlotte / Kriechbaumer, Verena / Bolanos-Garcia, Victor M

    Frontiers in physiology

    2022  Volume 13, Page(s) 938688

    Abstract: The Anaphase Promoting Complex (APC/C), a large cullin-RING E3-type ubiquitin ligase, constitutes the ultimate target of the Spindle Assembly Checkpoint (SAC), an intricate regulatory circuit that ensures the high fidelity of chromosome segregation in ... ...

    Abstract The Anaphase Promoting Complex (APC/C), a large cullin-RING E3-type ubiquitin ligase, constitutes the ultimate target of the Spindle Assembly Checkpoint (SAC), an intricate regulatory circuit that ensures the high fidelity of chromosome segregation in eukaryotic organisms by delaying the onset of anaphase until each chromosome is properly bi-oriented on the mitotic spindle. Cell-division cycle protein 20 homologue (CDC20) is a key regulator of APC/C function in mitosis. The formation of the APC/C
    Language English
    Publishing date 2022-07-25
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2564217-0
    ISSN 1664-042X
    ISSN 1664-042X
    DOI 10.3389/fphys.2022.938688
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  9. Article: The spindle checkpoint proteins BUB1 and BUBR1: (SLiM)ming down to the basics

    Elowe, Sabine / Bolanos-Garcia, Victor M.

    Trends in biochemical sciences. 2022 Apr., v. 47, no. 4

    2022  

    Abstract: Benzimidazole 1 (BUB1) and budding uninhibited by benzimidazole 1-related 1 (BUBR1) are multidomain paralogs with key roles in chromosome alignment during mitosis and the spindle assembly checkpoint (SAC), an evolutionarily conserved signaling pathway ... ...

    Abstract Benzimidazole 1 (BUB1) and budding uninhibited by benzimidazole 1-related 1 (BUBR1) are multidomain paralogs with key roles in chromosome alignment during mitosis and the spindle assembly checkpoint (SAC), an evolutionarily conserved signaling pathway that monitors errors in chromosome segregation during cell division in eukaryotes. Although BUB1 and BUBR1 share a similar domain organization and short linear interaction motifs (SLiMs), they control distinct aspects of chromosome congression and the SAC. Here we discuss the roles of BUB1 and BUBR1 SLiMs in mitosis and complement this with additional insights gleamed from studying their evolution. We show that BUB1 and BUBR1 SLiMs form highly specific interactions that are carefully orchestrated in space and time and contend that they define BUB1 and BUBR1 as organizing hubs that drive SAC signaling and ensure genome stability.
    Keywords benzimidazole ; chromosome segregation ; chromosomes ; eukaryotic cells ; evolution ; genome ; mitosis ; space and time
    Language English
    Dates of publication 2022-04
    Size p. 352-366.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 194220-7
    ISSN 0968-0004 ; 0376-5067
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2022.01.004
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 78/716: Show issues

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  10. Article ; Online: Identification of Novel Potential Heparanase Inhibitors Using Virtual Screening

    Alfredo Rus / Victor M. Bolanos-Garcia / Agatha Bastida / Paula Morales

    Catalysts, Vol 12, Iss 503, p

    2022  Volume 503

    Abstract: Heparanase (HPSE) is a mammalian endo-β-D-glucuronidase that cleaves heparan sulphate (HS) side chains of heparin sulphate proteoglycans (HSPG), a class of molecules composed of repeating polysulfated disaccharide units of glucosamine and hexuronic acid ... ...

    Abstract Heparanase (HPSE) is a mammalian endo-β-D-glucuronidase that cleaves heparan sulphate (HS) side chains of heparin sulphate proteoglycans (HSPG), a class of molecules composed of repeating polysulfated disaccharide units of glucosamine and hexuronic acid residues. HPSE controls the availability of growth factors, chemokines, lipoproteins and other bioactive molecules by degrading HS into smaller fractions, allowing the release of saccharide fragments that activate a plethora of signaling processes. HPSE overexpression has been correlated with tumor survival and metastasis as well as several diseases associated with chronic inflammation, including the ongoing COVID-19 pandemic caused by SARS-CoV-2. Thus, the search for molecules that could potentially inhibit HPSE has become increasingly relevant in the clinic. In this study, we have integrated a strategy that combines virtual screening and molecular docking of publicly available chemical databases to identify small compounds that can be developed into novel HPSE inhibitors. Structural rationalization of the interactions previously reported compounds led us to identify promising unexplored chemotypes. Here we show that these novel potential HPSE inhibitors present optimized in silico druggability and docking properties and may serve as pharmacological tools for the treatment of chronic and infectious diseases associated with chronic inflammation.
    Keywords COVID-19 ; docking ; heparanase (HPSE) ; inhibitors ; virtual screening ; Chemical technology ; TP1-1185 ; Chemistry ; QD1-999
    Subject code 540
    Language English
    Publishing date 2022-04-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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