These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Journal Abstract Search
402 related items for PubMed ID: 2096886
1. Binding of the soybean Bowman-Birk proteinase inhibitor and of its chymotrypsin and trypsin inhibiting fragments to bovine alpha-chymotrypsin and bovine beta-trypsin. A thermodynamic study. Ascenzi P, Amiconi G, Bolognesi M, Menegatti E, Guarneri M. J Mol Recognit; 1990; 3(5-6):192-6. PubMed ID: 2096886 [Abstract] [Full Text] [Related]
2. Binding of native and [homoserine lactone-52]-52,53-seco-bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor) to porcine pancreatic beta-kallikrein-B and bovine alpha-chymotrypsin: thermodynamic study. Oddone R, Barra D, Amiconi G, Ascenzi P, Tarricone C, Bolognesi M, Bortolotti F, Menegatti E. J Mol Recognit; 1994 Mar; 7(1):39-46. PubMed ID: 7527234 [Abstract] [Full Text] [Related]
4. Inhibition of bovine beta-trypsin, human alpha-thrombin and porcine pancreatic beta-kallikrein-B by benzamidine and its bis-, tris- and tetra-derivatives: thermodynamic and molecular modeling study. Menegatti E, Ferroni R, Nastruzzi C, Bortolotti F, Scalia S, Amiconi G, Bolognesi M, Coletta M, Onesti S, Fruttero R. Farmaco; 1991 Nov; 46(11):1297-310. PubMed ID: 1811616 [Abstract] [Full Text] [Related]
7. Binding of the recombinant proteinase inhibitor eglin c from leech Hirudo medicinalis to serine (pro)enzymes: a comparative thermodynamic study. Ascenzi P, Aducci P, Amiconi G, Ballio A, Guaragna A, Menegatti E, Schnebli HP, Bolognesi M. J Mol Recognit; 1991 Nov; 4(4):113-9. PubMed ID: 1799460 [Abstract] [Full Text] [Related]
8. Proteinase inhibition using small Bowman-Birk-type structures. Fernandez JH, Mello MO, Galgaro L, Tanaka AS, Silva-Filho MC, Neshich G. Genet Mol Res; 2007 Oct 05; 6(4):846-58. PubMed ID: 18058707 [Abstract] [Full Text] [Related]
9. Identification and characterization of a Bowman-Birk inhibitor active towards trypsin but not chymotrypsin in Lupinus albus seeds. Scarafoni A, Consonni A, Galbusera V, Negri A, Tedeschi G, Rasmussen P, Magni C, Duranti M. Phytochemistry; 2008 Jun 05; 69(9):1820-5. PubMed ID: 18474386 [Abstract] [Full Text] [Related]
10. [The classical Bowman-Birk soy inhibitor is an effective inhibitor of human granulocyte alpha-chymotrypsin and cathepsin G]. Gladysheva IP, Larionova NI, Gladyshev DP, Tikhonova TV, Kazanskaia NF. Biokhimiia; 1994 Apr 05; 59(4):513-8. PubMed ID: 8018773 [Abstract] [Full Text] [Related]
11. Binding of the Kunitz-type trypsin inhibitor DE-3 from Erythrina caffra seeds to serine proteinases: a comparative study. Onesti S, Matthews DJ, Aducci P, Amiconi G, Bolognesi M, Menegatti E, Ascenzi P. J Mol Recognit; 1992 Sep 05; 5(3):105-14. PubMed ID: 1298302 [Abstract] [Full Text] [Related]
16. Crystal structure of the Bowman-Birk inhibitor from barley seeds in ternary complex with porcine trypsin. Park EY, Kim JA, Kim HW, Kim YS, Song HK. J Mol Biol; 2004 Oct 08; 343(1):173-86. PubMed ID: 15381428 [Abstract] [Full Text] [Related]