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267 related items for PubMed ID: 25301953
1. Sequence and conformational specificity in substrate recognition: several human Kunitz protease inhibitor domains are specific substrates of mesotrypsin. Pendlebury D, Wang R, Henin RD, Hockla A, Soares AS, Madden BJ, Kazanov MD, Radisky ES. J Biol Chem; 2014 Nov 21; 289(47):32783-97. PubMed ID: 25301953 [Abstract] [Full Text] [Related]
2. Disulfide engineering of human Kunitz-type serine protease inhibitors enhances proteolytic stability and target affinity toward mesotrypsin. Cohen I, Coban M, Shahar A, Sankaran B, Hockla A, Lacham S, Caulfield TR, Radisky ES, Papo N. J Biol Chem; 2019 Mar 29; 294(13):5105-5120. PubMed ID: 30700553 [Abstract] [Full Text] [Related]
3. Determinants of affinity and proteolytic stability in interactions of Kunitz family protease inhibitors with mesotrypsin. Salameh MA, Soares AS, Navaneetham D, Sinha D, Walsh PN, Radisky ES. J Biol Chem; 2010 Nov 19; 285(47):36884-96. PubMed ID: 20861008 [Abstract] [Full Text] [Related]
4. The amyloid precursor protein/protease nexin 2 Kunitz inhibitor domain is a highly specific substrate of mesotrypsin. Salameh MA, Robinson JL, Navaneetham D, Sinha D, Madden BJ, Walsh PN, Radisky ES. J Biol Chem; 2010 Jan 15; 285(3):1939-49. PubMed ID: 19920152 [Abstract] [Full Text] [Related]
5. Mesotrypsin Has Evolved Four Unique Residues to Cleave Trypsin Inhibitors as Substrates. Alloy AP, Kayode O, Wang R, Hockla A, Soares AS, Radisky ES. J Biol Chem; 2015 Aug 28; 290(35):21523-35. PubMed ID: 26175157 [Abstract] [Full Text] [Related]
6. The P(2)' residue is a key determinant of mesotrypsin specificity: engineering a high-affinity inhibitor with anticancer activity. Salameh MA, Soares AS, Hockla A, Radisky DC, Radisky ES. Biochem J; 2011 Nov 15; 440(1):95-105. PubMed ID: 21806544 [Abstract] [Full Text] [Related]