<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Jmel MA</submitter><funding>National Institutes of Health</funding><funding>NIH HHS</funding><pagination>1556</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9865953</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>24(2)</volume><pubmed_abstract>Kunitz domain-containing proteins are ubiquitous serine protease inhibitors with promising therapeutic potential. They target key proteases involved in major cellular processes such as inflammation or hemostasis through competitive inhibition in a substrate-like manner. Protease inhibitors from the Kunitz superfamily have a low molecular weight (18-24 kDa) and are characterized by the presence of one or more Kunitz motifs consisting of α-helices and antiparallel β-sheets stabilized by three disulfide bonds. Kunitz-type inhibitors are an important fraction of the protease inhibitors found in tick saliva. Their roles in inhibiting and/or suppressing host homeostatic responses continue to be shown to be additive or synergistic with other protease inhibitors such as cystatins or serpins, ultim</pubmed_abstract><journal>International journal of molecular sciences</journal><pubmed_title>Tick Salivary Kunitz-Type Inhibitors: Targeting Host Hemostasis and Immunity to Mediate Successful Blood Feeding.</pubmed_title><pmcid>PMC9865953</pmcid><funding_grant_id>Z01 AI001337-01</funding_grant_id><pubmed_authors>Araujo RN</pubmed_authors><pubmed_authors>Jmel MA</pubmed_authors><pubmed_authors>Tirloni L</pubmed_authors><pubmed_authors>Sa-Nunes A</pubmed_authors><pubmed_authors>Voet H</pubmed_authors><pubmed_authors>Kotsyfakis M</pubmed_authors></additional><is_claimable>false</is_claimable><name>Tick Salivary Kunitz-Type Inhibitors: Targeting Host Hemostasis and Immunity to Mediate Successful Blood Feeding.</name><description>Kunitz domain-containing proteins are ubiquitous serine protease inhibitors with promising therapeutic potential. They target key proteases involved in major cellular processes such as inflammation or hemostasis through competitive inhibition in a substrate-like manner. Protease inhibitors from the Kunitz superfamily have a low molecular weight (18-24 kDa) and are characterized by the presence of one or more Kunitz motifs consisting of α-helices and antiparallel β-sheets stabilized by three disulfide bonds. Kunitz-type inhibitors are an important fraction of the protease inhibitors found in tick saliva. Their roles in inhibiting and/or suppressing host homeostatic responses continue to be shown to be additive or synergistic with other protease inhibitors such as cystatins or serpins, ultim</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Jan</publication><modification>2025-04-04T10:20:00.562Z</modification><creation>2025-02-19T00:12:50.808Z</creation></dates><accession>S-EPMC9865953</accession><cross_references><pubmed>36675071</pubmed><doi>10.3390/ijms24021556</doi></cross_references></HashMap>