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Characterization of a serine protease inhibitor from Trichinella spiralis and its participation in larval invasion of host's intestinal epithelial cells
Characterization of a serine protease inhibitor from Trichinella spiralis and its participation in larval invasion of host's intestinal epithelial cells
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Characterization of a serine protease inhibitor from Trichinella spiralis and its participation in larval invasion of host's intestinal epithelial cells

Song, Yan Yan ; Zhang, Yao ; Ren, Hua Nan ; Sun, Ge Ge ; Qi, Xin ; Yang, Fan ; Jiang, Peng ; Zhang, Xi ; Cui, Jing ; Wang, Zhong Quan

Parasites & vectors, 2018-09, Vol.11 (1), p.499-499, Article 499 [Periódico revisado por pares]

England: BioMed Central Ltd

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A new Piper nigrum cysteine proteinase inhibitor, PnCPI, with antifungal activity: molecular cloning, recombinant expression, functional analyses and molecular modeling
A new Piper nigrum cysteine proteinase inhibitor, PnCPI, with antifungal activity: molecular cloning, recombinant expression, functional analyses and molecular modeling
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A new Piper nigrum cysteine proteinase inhibitor, PnCPI, with antifungal activity: molecular cloning, recombinant expression, functional analyses and molecular modeling

Lima, Aline Medeiros ; Barros, Nicolle Louise Ferreira ; Freitas, Ana Camila Oliveira ; Tavares, Liliane Souza Conceição ; Pirovani, Carlos Priminho ; Siqueira, Andrei Santos ; Gonçalves, Evonnildo Costa ; de Souza, Cláudia Regina Batista

Planta, 2020-08, Vol.252 (2), p.16-16, Article 16 [Periódico revisado por pares]

Berlin/Heidelberg: Springer Berlin Heidelberg

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Human clade B serpins (ov-serpins) belong to a cohort of evolutionarily dispersed intracellular proteinase inhibitor clades that protect cells from promiscuous proteolysis
Human clade B serpins (ov-serpins) belong to a cohort of evolutionarily dispersed intracellular proteinase inhibitor clades that protect cells from promiscuous proteolysis
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Human clade B serpins (ov-serpins) belong to a cohort of evolutionarily dispersed intracellular proteinase inhibitor clades that protect cells from promiscuous proteolysis

Silverman, G A ; Whisstock, J C ; Askew, D J ; Pak, S C ; Luke, C J ; Cataltepe, S ; Irving, J A ; Bird, P I

Cellular and molecular life sciences : CMLS, 2004-02, Vol.61 (3), p.301-325 [Periódico revisado por pares]

Switzerland: Springer Nature B.V

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4
Proteinase inhibitors in legume herbivore defense: from natural to genetically engineered protectants
Proteinase inhibitors in legume herbivore defense: from natural to genetically engineered protectants
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Proteinase inhibitors in legume herbivore defense: from natural to genetically engineered protectants

Sultana, Mst Shamira ; Millwood, Reginald J. ; Mazarei, Mitra ; Stewart, C. Neal

Plant cell reports, 2022-02, Vol.41 (2), p.293-305 [Periódico revisado por pares]

Berlin/Heidelberg: Springer Berlin Heidelberg

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Cysteine protease inhibitor of Schistosoma japonicum - A parasite-derived negative immunoregulatory factor
Cysteine protease inhibitor of Schistosoma japonicum - A parasite-derived negative immunoregulatory factor
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Cysteine protease inhibitor of Schistosoma japonicum - A parasite-derived negative immunoregulatory factor

Chen, Lin ; He, Baohua ; Hou, Wei ; He, Li

Parasitology research (1987), 2017-03, Vol.116 (3), p.901-908 [Periódico revisado por pares]

Berlin/Heidelberg: Springer Berlin Heidelberg

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6
Expression of two barley proteinase inhibitors in tomato promotes endogenous defensive response and enhances resistance to Tuta absoluta
Expression of two barley proteinase inhibitors in tomato promotes endogenous defensive response and enhances resistance to Tuta absoluta
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Expression of two barley proteinase inhibitors in tomato promotes endogenous defensive response and enhances resistance to Tuta absoluta

Hamza, Rim ; Pérez-Hedo, Meritxell ; Urbaneja, Alberto ; Rambla, José L ; Granell, Antonio ; Gaddour, Kamel ; Beltrán, José P ; Cañas, Luis A

BMC plant biology, 2018-01, Vol.18 (1), p.24-24, Article 24 [Periódico revisado por pares]

England: BioMed Central Ltd

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SERPINE2 is an oral cancer-promoting factor that induces angiogenesis and lymphangiogenesis
SERPINE2 is an oral cancer-promoting factor that induces angiogenesis and lymphangiogenesis
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SERPINE2 is an oral cancer-promoting factor that induces angiogenesis and lymphangiogenesis

Sasahira, Tomonori ; Kurihara-Shimomura, Miyako ; Shimomura, Hiroyuki ; Kirita, Tadaaki

International journal of clinical oncology, 2021-10, Vol.26 (10), p.1831-1839 [Periódico revisado por pares]

Singapore: Springer Singapore

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8
Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression
Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression
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Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression

Kim, Ju Hee ; Lim, Sung Don ; Jang, Cheol Seong

Plant molecular biology, 2020-06, Vol.103 (3), p.235-252 [Periódico revisado por pares]

Dordrecht: Springer Netherlands

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9
Serine protease inhibitors in plants: nature’s arsenal crafted for insect predators
Serine protease inhibitors in plants: nature’s arsenal crafted for insect predators
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Serine protease inhibitors in plants: nature’s arsenal crafted for insect predators

Jamal, Farrukh ; Pandey, Prabhash K ; Singh, Dushyant ; Khan, M. Y

Phytochemistry reviews, 2013-03, Vol.12 (1), p.1-34 [Periódico revisado por pares]

Dordrecht: Springer-Verlag

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Molecular characterization of serine protease inhibitor isoform 3, SmSPI, from Schistosoma mansoni
Molecular characterization of serine protease inhibitor isoform 3, SmSPI, from Schistosoma mansoni
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Molecular characterization of serine protease inhibitor isoform 3, SmSPI, from Schistosoma mansoni

Pakchotanon, Pattarakul ; Molee, Patamaporn ; Nuamtanong, Supaporn ; Limpanont, Yanin ; Chusongsang, Phiraphol ; Limsomboon, Jareemate ; Chusongsang, Yupa ; Maneewatchararangsri, Santi ; Chaisri, Urai ; Adisakwattana, Poom

Parasitology research (1987), 2016-08, Vol.115 (8), p.2981-2994 [Periódico revisado por pares]

Berlin/Heidelberg: Springer Berlin Heidelberg

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