Výsledky vyhledávání - "Marjo, Suomalainen"

Akademický článek

Probiotic supplementation restores normal microbiota composition and function in antibiotic-treated and in caesarean-born infants

Autor: Katri Korpela, Anne Salonen, Outi Vepsäläinen, Marjo Suomalainen, Carolin Kolmeder, Markku Varjosalo, Sini Miettinen, Kaarina Kukkonen, Erkki Savilahti, Mikael Kuitunen, Willem M de Vos

Publikováno v: Microbiome, Vol 6, Iss 1, Pp 1-11 (2018)

Abstract Background Infants born by caesarean section or receiving antibiotics are at increased risk of developing metabolic, inflammatory and immunological diseases, potentially due to disruption of normal gut microbiota at a critical developmental

Externí odkaz: https://doaj.org/article/363b758cc2a34c6dbac8d831b1d8140c

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Human single-chain urokinase is activated by the omptins PgtE ofSalmonella entericaand Pla ofYersinia pestisdespite mutations of active site residues

Autor: Marjo Suomalainen, Carmen Buchrieser, Hanna M. Järvinen, Johanna Haiko, Tiira Johansson, Nisse Kalkkinen, Liisa Laakkonen, Timo K. Korhonen, Katri M. Juuti

Publikováno v: Molecular Microbiology. 89:507-517

Fibrinolysis is important in cell migration and tightly regulated by specific inhibitors and activators; of the latter, urokinase (uPA) associates with enhancement of cell migration. Active uPA is formed through cleavage of the single-chain uPA (scuP

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::94c6adaa3bd84b5938b7c4a0384f2c9a
https://doi.org/10.1111/mmi.12293

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Temperature-Induced Changes in the Lipopolysaccharide ofYersinia pestisAffect Plasminogen Activation by the Pla Surface Protease

Autor: Ritva Virkola, Otto Holst, Yuriy A. Knirel, Leandro Araujo Lobo, Klaus Brandenburg, Timo K. Korhonen, Marjo Suomalainen, Andrey P. Anisimov, Buko Lindner

Publikováno v: Infection and Immunity. 78:2644-2652

The Pla surface protease of Yersinia pestis activates human plasminogen and is a central virulence factor in bubonic and pneumonic plague. Pla is a transmembrane -barrel protein and member of the omptin family of outer membrane proteases which requir

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fce07c932226e757acbb3031c3c842c8
https://doi.org/10.1128/iai.01329-09

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Lack of O-antigen is essential for plasminogen activation by Yersinia pestis and Salmonella enterica

Autor: Ritva Virkola, Marjo Suomalainen, Otto Holst, Timo K. Korhonen, Ilkka M. Helander, Hannu Lång, Maini Kukkonen, Päivi Kyllönen, Kaarina Lähteenmäki

Publikováno v: Molecular Microbiology. 51:215-225

The O-antigen of lipopolysaccharide (LPS) is a virulence factor in enterobacterial infections, and the advantage of its genetic loss in the lethal pathogen Yersinia pestis has remained unresolved. Y. pestis and Salmonella enterica express beta-barrel

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8f6ae80074eaeee588ca5484ce22f622
https://doi.org/10.1046/j.1365-2958.2003.03817.x

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Protein regions important for plasminogen activation and inactivation of alpha2-antiplasmin in the surface protease Pla of Yersinia pestis

Autor: Maini Kukkonen, Nisse Kalkkinen, Marjo Suomalainen, Hannu Lång, Kaarina Lähteenmäki, Levente Emödy, Timo K. Korhonen

Publikováno v: Molecular Microbiology. 40:1097-1111

The plasminogen activator, surface protease Pla, of the plague bacterium Yersinia pestis is an important virulence factor that enables the spread of Y. pestis from subcutaneous sites into circulation. Pla-expressing Y. pestis and recombinant Escheric

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29da8f68e819c86f52e3bdbc562f3873
https://doi.org/10.1046/j.1365-2958.2001.02451.x

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Human single-chain urokinase is activated by the omptins PgtE of Salmonella enterica and Pla of Yersinia pestis despite mutations of active site residues

Autor: Hanna M, Järvinen, Liisa, Laakkonen, Johanna, Haiko, Tiira, Johansson, Katri, Juuti, Marjo, Suomalainen, Carmen, Buchrieser, Nisse, Kalkkinen, Timo K, Korhonen

Publikováno v: Molecular Microbiology
Molecular Microbiology, Wiley, 2013, 89 (3), pp.507-517. ⟨10.1111/mmi.12293⟩
Molecular Microbiology, 2013, 89 (3), pp.507-517. ⟨10.1111/mmi.12293⟩

International audience; Fibrinolysis is important in cell migration and tightly regulated by specific inhibitors and activators; of the latter, urokinase (uPA) associates with enhancement of cell migration. Active uPA is formed through cleavage of th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::a4502f4fa4f2463202bed6e9fbec91ad
https://hal-pasteur.archives-ouvertes.fr/pasteur-01336155

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Invited review: Breaking barriers--attack on innate immune defences by omptin surface proteases of enterobacterial pathogens

Autor: Johanna Haiko, Timo K. Korhonen, Marjo Suomalainen, Kaarina Lähteenmäki, Teija Ojala

Publikováno v: Innate immunity. 15(2)

The omptin family of Gram-negative bacterial transmembrane aspartic proteases comprises surface proteins with a highly conserved β-barrel fold but differing biological functions. The omptins OmpT of Escherichia coli, PgtE of Salmonella enterica, and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::057198fd10f4daddf5aaf221658c1062
https://pubmed.ncbi.nlm.nih.gov/19318417

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Using every trick in the book: the Pla surface protease of Yersinia pestis

Autor: Marjo, Suomalainen, Johanna, Haiko, Päivi, Ramu, Leandro, Lobo, Maini, Kukkonen, Benita, Westerlund-Wikström, Ritva, Virkola, Kaarina, Lähteenmäki, Timo K, Korhonen

Publikováno v: Advances in experimental medicine and biology. 603

The Pla surface protease of Yersinia pestis, encoded by the Y. pestis-specific plasmid pPCP1, is a versatile virulence factor. In vivo studies have shown that Pla is essential in the establishment of bubonic plague, and in vitro studies have demonstr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1d011bb9275e63d1b48c66000606224b
https://pubmed.ncbi.nlm.nih.gov/17966423

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Activation of pro-matrix metalloproteinase-9 and degradation of gelatin by the surface protease PgtE of Salmonella enterica serovar Typhimurium

Autor: Päivi Ramu, Kaarina Lähteenmäki, Ilkka Julkunen, Eva Bjur, Hanna Raukola, Maini Kukkonen, Timo K. Korhonen, Minja Miettinen, Marjo Suomalainen, Otto Holst, Leandro Araujo Lobo, Mikael Rhen

Publikováno v: International journal of medical microbiology : IJMM. 298(3-4)

Mammalian matrix metalloproteinases (MMPs) degrade collagen networks in extracellular matrices by cleaving collagen and its denatured form gelatin, and thus enhance migration of mammalian cells. The gastrointestinal pathogen Salmonella enterica survi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db9942b7b71fd1458c5d6567b2560756
https://pubmed.ncbi.nlm.nih.gov/17888724

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Using Every Trick in the Book: The Pla Surface Protease of Yersinia pestis

Autor: Kaarina Lähteenmäki, Marjo Suomalainen, Timo K. Korhonen, Ritva Virkola, Päivi Ramu, Leandro Araujo Lobo, Johanna Haiko, Benita Westerlund-Wikström, Maini Kukkonen

Publikováno v: Advances In Experimental Medicine And Biology ISBN: 9780387721231

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fe21654b332158d4a37256ec8d116b6d
https://doi.org/10.1007/978-0-387-72124-8_24

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