Results 31 to 40 of about 31,169 (289)

Widespread signatures of selection for secreted peptidases in a fungal plant pathogen

BMC Evolutionary Biology, 2018
Background Fungal plant pathogens secrete a large arsenal of hydrolytic enzymes during the course of infection, including peptidases. Secreted peptidases have been extensively studied for their role as effectors.
Parvathy Krishnan, Xin Ma, Bruce A. McDonald, Patrick C. Brunner   +3 more
doaj   +1 more source

Taxon-Specific Proteins of the Pathogenic Entamoeba Species E. histolytica and E. nuttalli

Frontiers in Cellular and Infection Microbiology, 2021
The human protozoan parasite Entamoeba histolytica can live in the human intestine for months or years without generating any symptoms in the host. For unknown reasons, amoebae can suddenly destroy the intestinal mucosa and become invasive. This can lead
Constantin König, Barbara Honecker, Ian W. Wilson, Gareth D. Weedall, Neil Hall, Neil Hall, Thomas Roeder, Thomas Roeder, Nahla Galal Metwally, Iris Bruchhaus, Iris Bruchhaus   +10 more
doaj   +1 more source

Peptidases and growth of Lactococcus lactis in milk [PDF]

, 1995
To gain a detailed understanding of the function of peptidases of Lactococcus lactis in growth in milk a set of 16 mutants was constructed lacking one or combinations of the following peptidases: PepO, PepN, PepC, PepT, PepXP.
Venema, G.,, Kok, J.,, Kunji, E.R.S.,, Poolman, B., Mierau, I., Mierau, I.,, Kok, J., Venema, G., Kunji, E.R.S., Poolman, B.,   +9 more
core   +2 more sources

Investigating and Annotating the Human Peptidome Profile from Urine under Normal Physiological Conditions

Proteomes
Examining the composition of the typical urinary peptidome and identifying the enzymes responsible for its formation holds significant importance, as it mirrors the normal physiological state of the human body.
Amr Elguoshy, Keiko Yamamoto, Yoshitoshi Hirao, Tomohiro Uchimoto, Kengo Yanagita, Tadashi Yamamoto   +5 more
doaj   +1 more source

Distributions of Extracellular Peptidases Across Prokaryotic Genomes Reflect Phylogeny and Habitat

Frontiers in Microbiology, 2019
Proteinaceous compounds are abundant forms of organic nitrogen in soil and aquatic ecosystems, and the rate of protein depolymerization, which is accomplished by a diverse range of microbial secreted peptidases, often limits nitrogen turnover in the ...
Trang T. H. Nguyen, David D. Myrold, Ryan S. Mueller   +2 more
doaj   +1 more source

PepO is a target of the two-component systems VicRK and CovR required for systemic virulence of Streptococcus mutans

Virulence, 2020
Streptococcus mutans , a cariogenic species, is often associated with cardiovascular infections. Systemic virulence of specific S. mutans serotypes has been associated with the expression of the collagen- and laminin-binding protein Cnm, which is ...
Lívia A. Alves, Tridib Ganguly, Érika N. Harth-Chú, Jessica Kajfasz, José A. Lemos, Jacqueline Abranches, Renata O. Mattos-Graner   +6 more
doaj   +1 more source

Genome mining for peptidases in heat-tolerant and mesophilic fungi and putative adaptations for thermostability

BMC Genomics, 2018
Background Peptidases (EC 3.4) consist of a large group of hydrolytic enzymes that catalyze the hydrolysis of proteins accounting for approximately 65% of the total worldwide enzyme production.
Tássio Brito de Oliveira, Cene Gostinčar, Nina Gunde-Cimerman, Andre Rodrigues   +3 more
doaj   +1 more source

Cysteine peptidases and their inhibitors in Tetranychus urticae: a comparative genomic approach

BMC Genomics, 2012
Background Cysteine peptidases in the two-spotted spider mite Tetranychus urticae are involved in essential physiological processes, including proteolytic digestion.
Santamaría María, Hernández-Crespo Pedro, Ortego Félix, Grbic Vojislava, Grbic Miodrag, Diaz Isabel, Martinez Manuel   +6 more
doaj   +1 more source

The Relevance of Thimet Oligopeptidase in the Regulation of Energy Metabolism and Diet-Induced Obesity

Biomolecules, 2020
Thimet oligopeptidase (EC 3.4.24.15; EP24.15; THOP1) is a potential therapeutic target, as it plays key biological functions in processing biologically functional peptides.
Mayara C. F. Gewehr, Alexandre A. S. Teixeira, Bruna A. C. Santos, Luana A. Biondo, Fábio C. Gozzo, Amanda M. Cordibello, Rosangela A. S. Eichler, Patrícia Reckziegel, Renée N. O. Da Silva, Nilton B. Dos Santos, Niels O. S. Camara, Angela Castoldi, Maria L. M. Barreto-Chaves, Camila S. Dale, Nathalia Senger, Joanna D. C. C. Lima, Marilia C. L. Seelaender, Aline C. Inada, Eliana H. Akamine, Leandro M. Castro, Alice C. Rodrigues, José C. Rosa Neto, Emer S. Ferro   +22 more
doaj   +1 more source

Allergenicity reduction of cow’s milk proteins using latex peptidases [PDF]

, 2019
The present study evaluated four laticifer fluids as a novel source of peptidases capable of hydrolyzing proteins in cow’s milk. The latex peptidases from Calotropis procera (CpLP), Cryptostegia grandiflora (CgLP), and Carica papaya (CapLP) were able to ...
Ramos, Márcio V., Docena, Guillermo H., Docena, Guillermo, Ary, Maria B., Freitas, Cleverson D. T., Rizzo, Gastón, Oliveira, Jefferson S., Oliveira, João P.B., Rizzo, Gaston Pascual, Oliveira, João P. B., Oliveira, Hermógenes D., Freitas, Cleverson D.T., Candreva, Ángela María   +12 more
core   +1 more source