Patthy L - Search Results

1

Expression, purification and characterization of the second Kunitz-type protease inhibitor domain of the human WFIKKN protein.

Nagy A, Trexler M, Patthy L. Nagy A, et al. Among authors: patthy l. Eur J Biochem. 2003 May;270(9):2101-7. doi: 10.1046/j.1432-1033.2003.03593.x. Eur J Biochem. 2003. PMID: 12709070 Free article.

2

Refined solution structure and ligand-binding properties of PDC-109 domain b. A collagen-binding type II domain.

Constantine KL, Madrid M, Bányai L, Trexler M, Patthy L, Llinás M. Constantine KL, et al. Among authors: patthy l. J Mol Biol. 1992 Jan 5;223(1):281-98. doi: 10.1016/0022-2836(92)90731-x. J Mol Biol. 1992. PMID: 1731074

3

Sequence-specific 1H NMR assignments and structural characterization of bovine seminal fluid protein PDC-109 domain b.

Constantine KL, Ramesh V, Bányai L, Trexler M, Patthy L, Llinás M. Constantine KL, et al. Among authors: patthy l. Biochemistry. 1991 Feb 12;30(6):1663-72. doi: 10.1021/bi00220a032. Biochemistry. 1991. PMID: 1993183

4

The collagen-binding site of type-II units of bovine seminal fluid protein PDC-109 and fibronectin.

Bányai L, Trexler M, Koncz S, Gyenes M, Sipos G, Patthy L. Bányai L, et al. Among authors: patthy l. Eur J Biochem. 1990 Nov 13;193(3):801-6. doi: 10.1111/j.1432-1033.1990.tb19403.x. Eur J Biochem. 1990. PMID: 2249694 Free article.

5

Chemical modification and nuclear magnetic resonance studies on human plasminogen kringle 4. Assignment of tyrosine and histidine resonances to specific residues in the sequence.

Trexler M, Bányai L, Patthy L, Pluck ND, Williams RJ. Trexler M, et al. Among authors: patthy l. Eur J Biochem. 1985 Oct 15;152(2):439-46. doi: 10.1111/j.1432-1033.1985.tb09216.x. Eur J Biochem. 1985. PMID: 2996892 Free article.

6

Analysis and identification of aromatic signals in the proton magnetic resonance spectrum of the kringle 4 fragment from human plasminogen.

De Marco A, Pluck ND, Bányai L, Trexler M, Laursen RA, Patthy L, Llinás M, Williams RJ. De Marco A, et al. Among authors: patthy l. Biochemistry. 1985 Jan 29;24(3):748-53. doi: 10.1021/bi00324a032. Biochemistry. 1985. PMID: 3994983

7

Folding autonomy of the kringle 4 fragment of human plasminogen.

Trexler M, Patthy L. Trexler M, et al. Among authors: patthy l. Proc Natl Acad Sci U S A. 1983 May;80(9):2457-61. doi: 10.1073/pnas.80.9.2457. Proc Natl Acad Sci U S A. 1983. PMID: 6302685 Free PMC article.

8

Residues Cys-1 and Cys-79 are not essential for refolding of reduced-denatured kringle 4 fragment of human plasminogen.

Trexler M, Patthy L. Trexler M, et al. Among authors: patthy l. Biochim Biophys Acta. 1984 Jun 28;787(3):275-80. doi: 10.1016/0167-4838(84)90320-0. Biochim Biophys Acta. 1984. PMID: 6329306

It was shown previously that the Cys-1-Cys-79 disulphide bond forms in the last step of refolding of kringle 4 and that this bond is not essential for the lysine-Sepharose affinity of the kringle 4 fragment (Trexler, M. and Patthy, L. (1983) Proc. Natl. Acad. Sci. U …

It was shown previously that the Cys-1-Cys-79 disulphide bond forms in the last step of refolding of kringle 4 and that this bond is not ess …

9

Kringles: modules specialized for protein binding. Homology of the gelatin-binding region of fibronectin with the kringle structures of proteases.

Patthy L, Trexler M, Váli Z, Bányai L, Váradi A. Patthy L, et al. FEBS Lett. 1984 Jun 4;171(1):131-6. doi: 10.1016/0014-5793(84)80473-1. FEBS Lett. 1984. PMID: 6373375 Free article.

10

Structure of the omega-aminocarboxylic acid-binding sites of human plasminogen. Arginine 70 and aspartic acid 56 are essential for binding of ligand by kringle 4.

Trexler M, Váli Z, Patthy L. Trexler M, et al. Among authors: patthy l. J Biol Chem. 1982 Jul 10;257(13):7401-6. J Biol Chem. 1982. PMID: 6919539 Free article. No abstract available.

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