Literature for inhibitor I13.008: inhibitor of trypsin and Hageman factor (Cucurbita maxima)
(Topics flags: S Structure. To select only the references relevant to a single topic, click the link above. See explanation.)
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Terron-Hernandez,J., Gomez-Velasco,H., Pinzon-Yaya,L., Hernandez-Santoyo,A., Garcia-Ramirez,B. and Rodriguez-Romero,A.
Understanding the structure and function of HPI, a rubber tree serine protease inhibitor, and its interaction with subtilisin
Biochem Biophys Res Commun763, 151801-151801. PubMed Europe PubMed DOI -
Rihs,H.P., Sander,I., Heimann,H., Meurer,U., Bruning,T. and Raulf,M.
The new latex allergen Hev b 15: IgE-binding properties of a recombinant serine protease inhibitor
J Investig Allergol Clin Immunol25, 160-162. PubMed Europe PubMed -
[YEAR:30-7-2002]Cai,M., Gong,Y.X., Wen,L. and Krishnamoorthi,R.
Correlation of binding-loop internal dynamics with stability and function in potato I inhibitor family: relative contributions of Arg(50) and Arg(52) in Cucurbita maxima trypsin inhibitor-V as studied by site-directed mutagenesis and NMR spectroscopy
Biochemistry41, 9572-9579. PubMed Europe PubMed DOI -
Zavodszky,M., Chen,C.W., Huang,J.K., Zolkiewski,M., Wen,L. and Krishnamoorthi,R.
Disulfide bond effects on protein stability: designed variants of Cucurbita maxima trypsin inhibitor-V
Protein Sci10, 149-160. PubMed Europe PubMed DOI -
Liu,J., Gong,Y., Prakash,O., Wen,L., Lee,I., Huang,J.K. and Krishnamoorthi,R.
NMR studies of internal dynamics of serine proteinase protein inhibitors: Binding region mobilities of intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor (CMTI)-III of the squash family and comparison with those of counterparts of CMTI-V of the potato I family
Protein Sci7, 132-141. PubMed Europe PubMed DOI -
[YEAR:16-4-1996]Cai,M., Huang,Y., Prakash,O., Wen,L., Dunkelbarger,S.P., Huang,J.K., Liu,J. and Krishnamoorthi,R.
Differential modulation of binding loop flexibility and stability by Arg50 and Arg52 in Cucurbita maxima trypsin inhibitor-V deduced by trypsin-catalyzed hydrolysis and NMR spectroscopy
Biochemistry35, 4784-4794. PubMed Europe PubMed DOI -
[YEAR:6-2-1996]Liu,J., Prakash,O., Cai,M., Gong,Y., Huang,Y., Wen,L., Wen,J.J., Huang,J.K. and Krishnamoorthi,R.
Solution structure and backbone dynamics of recombinant Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy
Biochemistry35, 1516-1524. PubMed Europe PubMed DOI -
[YEAR:24-9-1996]Liu,J., Prakash,O., Huang,Y., Wen,L., Wen,J.J., Huang,J.K. and Krishnamoorthi,R.
Internal mobility of reactive-site-hydrolyzed recombinant Cucurbita maxima trypsin inhibitor-V characterized by NMR spectroscopy: evidence for differential stabilization of newly formed C- and N-termini
Biochemistry35, 12503-12510. PubMed Europe PubMed DOI -
Cai,M., Gong,Y., Prakash,O. and Krishnamoorthi,R.
Reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor-V: function, thermodynamic stability, and NMR solution structure
Biochemistry34, 12087-12094. PubMed Europe PubMed DOI -
Cai,M., Gong,Y., Kao,J.L. and Krishnamoorthi,R.
Three-dimensional solution structure of Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy
Biochemistry34, 5201-5211. PubMed Europe PubMed S -
[YEAR:27-2-1995]Wen,L., Lee,I., Chen,G., Huang,J.K., Gong,Y. and Krishnamoorthi,R.
Changing the inhibitory specificity and function of Cucurbita maxima trypsin inhibitor-V by site-directed mutagenesis
Biochem Biophys Res Commun207, 897-902. PubMed Europe PubMed DOI
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