Literature for inhibitor I07.005: trypsin inhibitor CMTI-I (Cucurbita maxima)

(Topics flags: S Structure, I Inhibitor. To select only the references relevant to a single topic, click the link above. See explanation.)

2002

Thaimattam,R., Tykarska,E., Bierzynski,A., Sheldrick,G.M. and Jaskolski,M. Atomic resolution structure of squash trypsin inhibitor: unexpected metal coordination Acta Crystallogr D Biol Crystallogr (2002) 58, 1448-1461. PubMed Europe PubMed DOI S

2000

[YEAR:23-5-2000]Grzesiak,A., Buczek,O., Petry,I., Szewczuk,Z. and Otlewski,J. Inhibition of serine proteinases from human blood clotting system by squash inhibitor mutants Biochim Biophys Acta (23-5-2000) 1478, 318-324. PubMed Europe PubMed DOI
[YEAR:5-3-2000]Lesner,A., Brzozowski,K., Kupryszewski,G. and Rolka,K. Design, chemical synthesis and kinetic studies of trypsin chromogenic substrates based on the proteinase binding loop of Cucurbita maxima trypsin inhibitor (CMTI-III) Biochem Biophys Res Commun (5-3-2000) 269, 81-84. PubMed Europe PubMed DOI
Zhukov,I., Jaroszewski,L. and Bierzynski,A. Conservative mutation Met8 - > Leu affects the folding process and structural stability of squash trypsin inhibitor CMTI-I Protein Sci (2000) 9, 273-279. PubMed Europe PubMed DOI PMC EPMC

1999

Helland,R., Berglund,G.I., Otlewski,J., Apostoluk,W., Andersen,O.A., Willassen,N.P. and Smalas,A.O. High-resolution structures of three new trypsin-squash-inhibitor complexes: a detailed comparison with other trypsins and their complexes Acta Crystallogr D Biol Crystallogr (1999) 55, 139-148. PubMed Europe PubMed DOI S

1995

[YEAR:18-12-1995]Bolewska,K., Krowarsch,D., Otlewski,J., Jaroszewski,L. and Bierzynski,A. Synthesis, cloning and expression in Escherichia coli of a gene coding for the Met8 - >Leu CMTI I - a representative of the squash inhibitors of serine proteinases FEBS Lett (18-12-1995) 377, 172-174. PubMed Europe PubMed DOI

1994

[YEAR:11-1-1994]Otlewski,J. and Zbyryt,T. Single peptide bond hydrolysis/resynthesis in squash inhibitors of serine proteinases. 1. Kinetics and thermodynamics of the interaction between squash inhibitors and bovine beta-trypsin Biochemistry (11-1-1994) 33, 200-207. PubMed Europe PubMed

1992

[YEAR:2-6-1992]Krishnamoorthi,R., Lin,C.L. and VanderVelde,D. Structural consequences of the natural substitution, E9K, on reactive-site-hydrolyzed squash (Cucurbita maxima) trypsin inhibitor (CMTI), as studied by two-dimensional NMR Biochemistry (2-6-1992) 31, 4965-4969. PubMed Europe PubMed DOI

1991

Nilges,M., Habazettl,J., Brunger,A.T. and Holak,T.A. Relaxation matrix refinement of the solution structure of squash trypsin inhibitor J Mol Biol (1991) 219, 499-510. PubMed Europe PubMed S

1990

Dryjanski,M., Otlewski,J., Polanowski,A. and Wilusz,T. Serine proteinase from Cucurbita ficifolia seed; purification, properties, substrate specificity and action on native squash trypsin inhibitor (CMTI I) Biol Chem Hoppe Seyler (1990) 371, 889-895. PubMed Europe PubMed I

1989

[YEAR:2-1-1989]Bode,W., Greyling,H.J., Huber,R., Otlewski,J. and Wilusz,T. The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes FEBS Lett (2-1-1989) 242, 285-292. PubMed Europe PubMed S