Results 21 to 30 of about 5,618 (220)

Interaction of subtilisins with serpins [PDF]

open access: yesProtein Science, 1996
AbstractSerpins are well‐characterized inhibitors of the chymotrypsin family serine proteinases. We have investigated the interaction of two serpins with members of the subtilisin family, proteinases that possess a similar catalytic mechanism to the chymotrypsins, but a totally different scaffold.
T, Komiyama   +3 more
openaire   +2 more sources

Mycosin-1, a subtilisin-like serine protease of Mycobacterium tuberculosis, is cell wall-associated and expressed during infection of macrophages

open access: yesBMC Microbiology, 2002
Background Exported proteases are commonly associated with virulence in bacterial pathogens, yet there is a paucity of information regarding their role in Mycobacterium tuberculosis.
Ehlers Mario RW   +4 more
doaj   +1 more source

Identification of functionally important microRNAs from rice inflorescence at heading stage of a qDTY4.1-QTL bearing Near Isogenic Line under drought conditions. [PDF]

open access: yesPLoS ONE, 2017
A cross between IR64 (high-yielding but drought-susceptible) and Aday Sel (drought-tolerant) rice cultivars yielded a stable line with enhanced grain yield under drought screening field trials at International Rice Research Institute.
Boon Huat Cheah   +4 more
doaj   +1 more source

Development of Versatile Vectors for Heterologous Expression in Bacillus

open access: yesMicroorganisms, 2018
The discovery of new enzymes for industrial application relies on a robust discovery pipeline. Such a pipeline should facilitate efficient molecular cloning, recombinant expression and functional screening procedures.
Øivind Larsen   +1 more
doaj   +1 more source

Treatment of wool fibres with subtilisin and subtilisin-PEG [PDF]

open access: yesEnzyme and Microbial Technology, 2005
Abstract In this work the diffusion of serine proteases into wool fabrics and yarns was studied. The proteases used were free subtilisin and subtilisin-PEG (the same enzyme that was covalently cross linked to polyethylene glycol). It is shown that the adsorption and diffusion is facilitated by the pre-treatment performed, being the alkaline ...
Silva, Carla J. S. M.   +3 more
openaire   +2 more sources

Revisiting Vitis vinifera subtilase gene family: a possible role in grapevine resistance against Plasmopara viticola

open access: yesFrontiers in Plant Science, 2016
Subtilisin-like proteases, also known as subtilases, are a very diverse family of serine peptidases present in many organisms. In grapevine, there are hints of the involvement of subtilases in defence mechanisms, but their role is not yet understood. The
Joana Figueiredo   +11 more
doaj   +1 more source

Transcription of Bacillus subtilis subtilisin and expression of subtilisin in sporulation mutants [PDF]

open access: yesJournal of Bacteriology, 1988
The start point for transcription of the subtilisin (aprE) gene was determined by primer extension analysis and was found to be at a point significantly different from that identified in a previously published report (S. L. Wong, C. W. Price, D. S. Goldfarb, and R. H. Doi, Proc. Natl. Acad. Sci. USA 81:1184-1188, 1984).
E, Ferrari   +3 more
openaire   +2 more sources

Cross genome comparisons of serine proteases in Arabidopsis and rice

open access: yesBMC Genomics, 2006
Background Serine proteases are one of the largest groups of proteolytic enzymes found across all kingdoms of life and are associated with several essential physiological pathways.
Sowdhamini R, Tripathi Lokesh P
doaj   +1 more source

Structure-function analysis of Sedolisins: evolution of tripeptidyl peptidase and endopeptidase subfamilies in fungi

open access: yesBMC Bioinformatics, 2018
Background Sedolisins are acid proteases that are related to the basic subtilisins. They have been identified in all three superkingdoms but are not ubiquitous, although fungi that secrete acids as part of their lifestyle can have up to six paralogs ...
Facundo Orts, Arjen ten Have
doaj   +1 more source

Crystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg [PDF]

open access: yesEuropean Journal of Biochemistry, 1998
The crystal structure of subtilisin DY inhibited by N‐benzyloxycarbonyl‐Ala‐Pro‐Phe‐chloromethyl ketone has been solved by molecular replacement with subtilisin Carlsberg as the starting model. The model has been refined to a crystallographic R factor (= Σ∣∣Fo∣−∣Fc∣∣ / Σ∣Fo∣) of 15.1 % using X‐ray diffraction data to 0.175 nm resolution.
S, Eschenburg   +6 more
openaire   +2 more sources

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