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  1. Article ; Online: In Search of Spectroscopic Signatures of Periodontitis: A SERS-Based Magnetomicrofluidic Sensor for Detection of

    Witkowska, Evelin / Łasica, Anna M / Niciński, Krzysztof / Potempa, Jan / Kamińska, Agnieszka

    ACS sensors

    2021  Volume 6, Issue 4, Page(s) 1621–1635

    Abstract: Recently, ...

    Abstract Recently,
    MeSH term(s) Aggregatibacter actinomycetemcomitans ; Humans ; Periodontitis/diagnosis ; Porphyromonas gingivalis
    Language English
    Publishing date 2021-04-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2379-3694
    ISSN (online) 2379-3694
    DOI 10.1021/acssensors.1c00166
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Influence of Environmental and Genetic Factors on Proteomic Profiling of Outer Membrane Vesicles from

    Godlewska, Renata / Klim, Joanna / Dębski, Janusz / Wyszyńska, Agnieszka / Łasica, Anna

    Polish journal of microbiology

    2019  Volume 68, Issue 2, Page(s) 255–261

    Abstract: The proteomes of outer membrane vesicles (OMVs) secreted by : The proteomes of outer membrane vesicles (OMVs) secreted ... ...

    Abstract The proteomes of outer membrane vesicles (OMVs) secreted by
    The proteomes of outer membrane vesicles (OMVs) secreted by
    MeSH term(s) Anti-Bacterial Agents/pharmacology ; Bacterial Proteins/analysis ; Campylobacter jejuni/chemistry ; Campylobacter jejuni/drug effects ; Campylobacter jejuni/genetics ; Extracellular Vesicles/chemistry ; Gene Deletion ; Heat-Shock Proteins/deficiency ; Oxidoreductases/deficiency ; Oxygen/toxicity ; Proteome/analysis ; Stress, Physiological
    Chemical Substances Anti-Bacterial Agents ; Bacterial Proteins ; Heat-Shock Proteins ; Proteome ; Oxidoreductases (EC 1.-) ; Oxygen (S88TT14065)
    Language English
    Publishing date 2019-06-12
    Publishing country Poland
    Document type Journal Article
    ZDB-ID 2234080-4
    ISSN 2544-4646 ; 1733-1331
    ISSN (online) 2544-4646
    ISSN 1733-1331
    DOI 10.33073/pjm-2019-027
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: The Type IX Secretion System (T9SS): Highlights and Recent Insights into Its Structure and Function.

    Lasica, Anna M / Ksiazek, Miroslaw / Madej, Mariusz / Potempa, Jan

    Frontiers in cellular and infection microbiology

    2017  Volume 7, Page(s) 215

    Abstract: Protein secretion systems are vital for prokaryotic life, as they enable bacteria to acquire nutrients, communicate with other species, defend against biological and chemical agents, and facilitate disease through the delivery of virulence factors. In ... ...

    Abstract Protein secretion systems are vital for prokaryotic life, as they enable bacteria to acquire nutrients, communicate with other species, defend against biological and chemical agents, and facilitate disease through the delivery of virulence factors. In this review, we will focus on the recently discovered type IX secretion system (T9SS), a complex translocon found only in some species of the
    MeSH term(s) Bacterial Proteins/metabolism ; Bacterial Secretion Systems/chemistry ; Bacterial Secretion Systems/physiology ; Bacteroidetes/physiology ; Flavobacterium/physiology ; Humans ; Porphyromonas gingivalis/pathogenicity ; Porphyromonas gingivalis/physiology ; Protein Processing, Post-Translational ; Protein Transport ; Virulence Factors
    Chemical Substances Bacterial Proteins ; Bacterial Secretion Systems ; Virulence Factors
    Language English
    Publishing date 2017-05-26
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2619676-1
    ISSN 2235-2988 ; 2235-2988
    ISSN (online) 2235-2988
    ISSN 2235-2988
    DOI 10.3389/fcimb.2017.00215
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Structural determinants of inhibition of Porphyromonas gingivalis gingipain K by KYT-36, a potent, selective, and bioavailable peptidase inhibitor.

    Guevara, Tibisay / Rodríguez-Banqueri, Arturo / Lasica, Anna M / Ksiazek, Miroslaw / Potempa, Barbara A / Potempa, Jan / Gomis-Rüth, F Xavier

    Scientific reports

    2019  Volume 9, Issue 1, Page(s) 4935

    Abstract: Porphyromonas gingivalis is a member of the dysbiotic oral microbiome and a "keystone pathogen" that causes severe periodontal disease, which is among the most prevalent infectious diseases. Part of the virulence factors secreted by P. gingivalis are the ...

    Abstract Porphyromonas gingivalis is a member of the dysbiotic oral microbiome and a "keystone pathogen" that causes severe periodontal disease, which is among the most prevalent infectious diseases. Part of the virulence factors secreted by P. gingivalis are the essential cysteine peptidases gingipain K (Kgp) and R (RgpA and RgpB), which account for 85% of the extracellular proteolytic activity of the pathogen and are thus prime targets for inhibition. We report the high-resolution (1.20 Å) complex structure of Kgp with KYT-36, a peptide-derived, potent, bioavailable and highly selective inhibitor, which is widely used for studies in vitro, in cells and in vivo. Sub-nanomolar inhibition of Kgp is achieved by tight binding to the active-site cleft, which is covered for its sub-sites S
    MeSH term(s) Bacteroidaceae Infections/drug therapy ; Bacteroidaceae Infections/microbiology ; Benzylamines/chemistry ; Benzylamines/pharmacology ; Benzylamines/therapeutic use ; Carbamates/chemistry ; Carbamates/pharmacology ; Carbamates/therapeutic use ; Catalytic Domain/drug effects ; Crystallography, X-Ray ; Drug Development ; Gingipain Cysteine Endopeptidases/antagonists & inhibitors ; Gingipain Cysteine Endopeptidases/metabolism ; Gingipain Cysteine Endopeptidases/ultrastructure ; Hydrazines/chemistry ; Hydrazines/pharmacology ; Hydrazines/therapeutic use ; Hydrophobic and Hydrophilic Interactions ; Periodontitis/drug therapy ; Periodontitis/microbiology ; Porphyromonas gingivalis/metabolism ; Porphyromonas gingivalis/pathogenicity ; Porphyromonas gingivalis/ultrastructure ; Protease Inhibitors/chemistry ; Protease Inhibitors/pharmacology ; Protease Inhibitors/therapeutic use ; Protein Domains ; Structure-Activity Relationship ; Virulence Factors/antagonists & inhibitors ; Virulence Factors/metabolism
    Chemical Substances Benzylamines ; Carbamates ; Gingipain Cysteine Endopeptidases ; Hydrazines ; KYT-36 ; Protease Inhibitors ; Virulence Factors
    Language English
    Publishing date 2019-03-20
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-019-41354-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: PorZ, an Essential Component of the Type IX Secretion System of

    Madej, Mariusz / Nowakowska, Zuzanna / Ksiazek, Miroslaw / Lasica, Anna M / Mizgalska, Danuta / Nowak, Magdalena / Jacula, Anna / Bzowska, Monika / Scavenius, Carsten / Enghild, Jan J / Aduse-Opoku, Joseph / Curtis, Michael A / Gomis-Rüth, F Xavier / Potempa, Jan

    mBio

    2021  Volume 12, Issue 1

    Abstract: Cargo proteins of the type IX secretion system (T9SS) in human pathogens from the Bacteroidetes phylum invariably possess a conserved C-terminal domain (CTD) that functions as a signal for outer membrane (OM) translocation. ... ...

    Abstract Cargo proteins of the type IX secretion system (T9SS) in human pathogens from the Bacteroidetes phylum invariably possess a conserved C-terminal domain (CTD) that functions as a signal for outer membrane (OM) translocation. In
    MeSH term(s) Aminoacyltransferases/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Bacterial Secretion Systems/genetics ; Bacterial Secretion Systems/metabolism ; Cysteine Endopeptidases/metabolism ; Lipopolysaccharides/metabolism ; Peptidyl Transferases/genetics ; Peptidyl Transferases/metabolism ; Porphyromonas gingivalis/enzymology ; Porphyromonas gingivalis/genetics ; Porphyromonas gingivalis/metabolism ; Protein Binding ; Protein Processing, Post-Translational ; Protein Transport
    Chemical Substances Bacterial Proteins ; Bacterial Secretion Systems ; Lipopolysaccharides ; Aminoacyltransferases (EC 2.3.2.-) ; sortase A (EC 2.3.2.-) ; Peptidyl Transferases (EC 2.3.2.12) ; Cysteine Endopeptidases (EC 3.4.22.-)
    Language English
    Publishing date 2021-02-23
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mBio.02262-20
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Enhancement of direct electron transfer in graphene bioelectrodes containing novel cytochrome c

    Izzo, Miriam / Osella, Silvio / Jacquet, Margot / Kiliszek, Małgorzata / Harputlu, Ersan / Starkowska, Alicja / Łasica, Anna / Unlu, C Gokhan / Uśpieński, Tomasz / Niewiadomski, Paweł / Bartosik, Dariusz / Trzaskowski, Bartosz / Ocakoglu, Kasim / Kargul, Joanna

    Bioelectrochemistry (Amsterdam, Netherlands)

    2021  Volume 140, Page(s) 107818

    Abstract: The highly efficient bioelectrodes based on single layer graphene (SLG) functionalized with pyrene self-assembled monolayer and novel ... ...

    Abstract The highly efficient bioelectrodes based on single layer graphene (SLG) functionalized with pyrene self-assembled monolayer and novel cytochromec
    MeSH term(s) Amino Acid Sequence ; Cytochrome c Group/chemistry ; Cytochrome c Group/genetics ; Electrodes ; Electron Transport ; Graphite/chemistry ; Heme ; Mutation
    Chemical Substances Cytochrome c Group ; cytochrome c553 ; Heme (42VZT0U6YR) ; Graphite (7782-42-5)
    Language English
    Publishing date 2021-04-08
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 2010650-6
    ISSN 1878-562X ; 0302-4598 ; 1567-5394
    ISSN (online) 1878-562X
    ISSN 0302-4598 ; 1567-5394
    DOI 10.1016/j.bioelechem.2021.107818
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Zastosowanie mikroorganizmów jako wektorów w antynowotworowych terapiach genowych.

    Łepeta, Katarzyna / Łasica, Anna Maria / Jagusztyn-Krynicka, Elzbieta Katarzyna

    Postepy biochemii

    2012  Volume 58, Issue 3, Page(s) 314–326

    Abstract: Gene therapy represents a potential new strategy for cancer treatment. In order to deliver a transgene into target tumor cells, a vector system is required. To date, most of the cancer therapies are based on the use of different viral vectors. However, ... ...

    Title translation Application of microorganisms as delivery vehicles in cancer gene therapies.
    Abstract Gene therapy represents a potential new strategy for cancer treatment. In order to deliver a transgene into target tumor cells, a vector system is required. To date, most of the cancer therapies are based on the use of different viral vectors. However, bacteria such as Salmonella, Clostridium or non-pathogenic Bifidobacterium can selectively accumulate in tumors in vivo what renders them useful for cancer gene therapy vectors. Although the mechanism of DNA transfer from bacteria to mammalian cells is not completely understood their potential to deliver therapeutic genes into tumor cells have been demonstrated in vitro and in vivo. The review presents recent achievements in bacteria-mediated cancer gene therapy.
    MeSH term(s) Animals ; Gene Transfer Techniques ; Genetic Therapy/methods ; Genetic Vectors ; Humans ; Neoplasms/genetics ; Neoplasms/therapy ; Transformation, Bacterial
    Language Polish
    Publishing date 2012
    Publishing country Poland
    Document type English Abstract ; Journal Article ; Review
    ZDB-ID 414019-9
    ISSN 0032-5422
    ISSN 0032-5422
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Porphyromonas gingivalis genes conferring fitness in a tobacco-rich environment.

    Hutcherson, Justin A / Gogenini, Himabindu / Lamont, Gwyneth J / Miller, Daniel P / Nowakowska, Zuzanna / Lasica, Anna M / Liu, Chengcheng / Potempa, Jan / Lamont, Richard J / Yoder-Himes, Deborah / Scott, David A

    Molecular oral microbiology

    2019  Volume 35, Issue 1, Page(s) 10–18

    Abstract: Smokers are more likely than non-smokers to harbour Porphyromonas gingivalis, they are more susceptible to destructive periodontal disease and smokers may, ultimately, benefit from tobacco-specific preventive and treatment strategies. A Mariner ... ...

    Abstract Smokers are more likely than non-smokers to harbour Porphyromonas gingivalis, they are more susceptible to destructive periodontal disease and smokers may, ultimately, benefit from tobacco-specific preventive and treatment strategies. A Mariner transposon insertion library for P. gingivalis ATCC 33277 was exploited to define 256 genes as essential for P. gingivalis survival in a tobacco-rich environment. Genes whose products play roles in protein transport and catabolism, nicotinamide processing, protection against oxidative stress, drug resistance, and transcriptional regulation have all been identified as essential for CSE survival. Many of these tobacco-essential genes are also requisite for epithelial colonization and abscess formation, suggestive of a core stress-related P. gingivalis genome. Single-gene deletions in several of the TnSeq-implicated genes led to significantly reduced P. gingivalis fitness upon competition with the parent strain, under conditions of cigarette smoke extract-induced stress (1,000 ng/ml nicotine equivalents). This study identifies, for the first time, a subset of P. gingivalis genes required for surviving the plethora of insults present in cigarette smoke. Such conditionally essential genes may delineate bacterial persistence strategies and represent novel therapeutic foci for the prevention of P. gingivalis infection and related diseases in smokers and in general.
    MeSH term(s) Gene Library ; Genes, Essential ; Humans ; Periodontal Diseases ; Porphyromonas gingivalis/genetics ; Nicotiana
    Language English
    Publishing date 2019-12-18
    Publishing country Denmark
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2537726-7
    ISSN 2041-1014 ; 2041-1006
    ISSN (online) 2041-1014
    ISSN 2041-1006
    DOI 10.1111/omi.12273
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: The role of Dsb proteins of Gram-negative bacteria in the process of pathogenesis

    Łasica, Anna M / Jagusztyn-Krynicka, Elżbieta K

    FEMS microbiology reviews. 2007 Sept., v. 31, no. 5

    2007  

    Abstract: Tertiary and quaternary structures of extracytoplasmic proteins containing more than one cysteine residue often require introduction of disulfide bonds. This process takes place in an oxidative environment, such as the periplasm of Gram-negative bacteria, ...

    Abstract Tertiary and quaternary structures of extracytoplasmic proteins containing more than one cysteine residue often require introduction of disulfide bonds. This process takes place in an oxidative environment, such as the periplasm of Gram-negative bacteria, and is catalyzed by Dsb (disulfide bond formation) proteins. Mutations in dsb genes influence the conformation and stability of many extracytoplasmic proteins. Thus, many pathogens become partially or fully attenuated due to improper folding of proteins that act as virulence factors. This review summarizes the current knowledge on Dsb proteins and their effect on the pathogenicity of Gram-negative bacteria. The potential application of Dsb proteins in biotechnology is also discussed.
    Keywords protein folding ; pathogenesis ; virulence
    Language English
    Dates of publication 2007-09
    Size p. 626-636.
    Publisher Blackwell Publishing Ltd
    Publishing place Oxford, UK
    Document type Article
    ZDB-ID 283740-7
    ISSN 1574-6976 ; 0168-6445
    ISSN (online) 1574-6976
    ISSN 0168-6445
    DOI 10.1111/j.1574-6976.2007.00081.x
    Database NAL-Catalogue (AGRICOLA)

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  10. Article: The role of Dsb proteins of Gram-negative bacteria in the process of pathogenesis.

    Łasica, Anna M / Jagusztyn-Krynicka, Elzbieta K

    FEMS microbiology reviews

    2007  Volume 31, Issue 5, Page(s) 626–636

    Abstract: Tertiary and quaternary structures of extracytoplasmic proteins containing more than one cysteine residue often require introduction of disulfide bonds. This process takes place in an oxidative environment, such as the periplasm of Gram-negative bacteria, ...

    Abstract Tertiary and quaternary structures of extracytoplasmic proteins containing more than one cysteine residue often require introduction of disulfide bonds. This process takes place in an oxidative environment, such as the periplasm of Gram-negative bacteria, and is catalyzed by Dsb (disulfide bond formation) proteins. Mutations in dsb genes influence the conformation and stability of many extracytoplasmic proteins. Thus, many pathogens become partially or fully attenuated due to improper folding of proteins that act as virulence factors. This review summarizes the current knowledge on Dsb proteins and their effect on the pathogenicity of Gram-negative bacteria. The potential application of Dsb proteins in biotechnology is also discussed.
    MeSH term(s) Bacterial Proteins/metabolism ; Gram-Negative Bacteria/chemistry ; Gram-Negative Bacteria/pathogenicity ; Membrane Proteins/metabolism ; Protein Folding ; Virulence Factors/metabolism
    Chemical Substances Bacterial Proteins ; Membrane Proteins ; Virulence Factors
    Language English
    Publishing date 2007-09
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 283740-7
    ISSN 1574-6976 ; 0168-6445
    ISSN (online) 1574-6976
    ISSN 0168-6445
    DOI 10.1111/j.1574-6976.2007.00081.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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