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Recent publications

Articles

1.   Cho HJ, Park HJ, Trexler M, Venselaar H, Lee KY, Robertson NG, Baek JI, Kang BS, Morton CC, Vriend G, Patthy L and Kim UK (2012) [22610276]
  A novel COCH mutation associated with autosomal dominant nonsyndromic hearing loss disrupts the structural stability of the vWFA2 domain.
  J Mol Med 90, 1321-31
2.   Kondás K, Szláma G, Nagy A, Trexler M and Patthy L (2011) [21936825]
  Biological functions of the WAP domain-containing multidomain proteins WFIKKN1 and WFIKKN2.
  Biochem Soc T 39, 1416-20
3.   Nagy A , Szláma Gy , Szarka E , Trexler M , Bányai L and Patthy L (2011) [-100077786]
  Reassessing Domain Architecture Evolution of Metazoan Proteins: Major Impact of Gene Prediction Errors
  Genes 2, 449-501
4.   Szláma G, Kondás K, Trexler M and Patthy L (2010) [21054789]
  WFIKKN1 and WFIKKN2 bind growth factors TGFβ1, BMP2 and BMP4 but do not inhibit their signalling activity.
  FEBS J 277, 5040-50
5.   Kondás K, Szláma G, Trexler M and Patthy L (2008) [18596030]
  Both WFIKKN1 and WFIKKN2 Have High Affinity for Growth and Differentiation Factors 8 and 11.
  J Biol Chem 283, 23677-84
6.   Ozhogina OA, Grishaev A, Bominaar EL, Patthy L, Trexler M and Llinás M (2008) [18956887]
  NMR solution structure of the neurotrypsin Kringle domain.
  Biochemistry-us 47, 12290-8
7.   Nagy I, Trexler M and Patthy L (2008) [19013156]
  The second von Willebrand type A domain of cochlin has high affinity for type I, type II and type IV collagens.
  FEBS Lett 582, 4003-7
8.   Liepinsh E, Nagy A, Trexler M, Patthy L and Otting G (2006) [16791741]
  Second Kunitz-type protease inhibitor domain of the human WFIKKN1 protein.
  J Biomol NMR 35, 73-8
9.   Jani M, Tordai H, Trexler M, Bányai L and Patthy L (2005) [15781326]
  Hydroxamate-based peptide inhibitors of matrix metalloprotease 2.
  Biochimie 87, 385-92
10.   Nagy I, Horváth M, Trexler M, Répássy G and Patthy L (2004) [14729849]
  A novel COCH mutation, V104del, impairs folding of the LCCL domain of cochlin and causes progressive hearing loss.
  Journal of Medical Genetics 41, e9
11.   Patthy L, Nagy I, Horváth M, Trexler M and Répássy G (2004) [15176382]
  Gene Symbol: COCH. Disease: DFNA9.
  Hum Genet 114, 607
12.   Nagy I, Trexler M and Patthy L (2003) [12615070]
  Expression and characterization of the olfactomedin domain of human myocilin.
  Biochem Bioph Res Co 302, 554-61
13.   Nagy A, Trexler M and Patthy L (2003) [12709070]
  Expression, purification and characterization of the second Kunitz-type protease inhibitor domain of the human WFIKKN protein.
  Eur J Biochem 270, 2101-7
14.   Liepinsh E, Banyai L, Pintacuda G, Trexler M, Patthy L and Otting G (2003) [12670942]
  NMR structure of the netrin-like domain (NTR) of human type I procollagen C-proteinase enhancer defines structural consensus of NTR domains and assesses potential proteinase inhibitory activity and ligand binding.
  J Biol Chem 278, 25982-9
15.   Trexler M, Briknarová K, Gehrmann M, Llinás M and Patthy L (2003) [12486137]
  Peptide ligands for the fibronectin type II modules of matrix metalloproteinase 2 (MMP-2).
  J Biol Chem 278, 12241-6
16.   Trexler M, Bányai L and Patthy L (2002) [11928817]
  Distinct expression pattern of two related human proteins containing multiple types of protease-inhibitory modules.
  Biol Chem 383, 223-8
17.   Roszmusz E, Patthy A, Trexler M and Patthy L (2002) [12147243]
  Structural characterization of the second TSP1-module of human thrombospondin.
  Biochem Bioph Res Co 296, 156-60
18.   Trexler M, Bányai L and Patthy L (2001) [11274388]
  A human protein containing multiple types of protease-inhibitory modules.
  P Natl Acad Sci Usa 98, 3705-9
19.   Roszmusz E, Patthy A, Trexler M and Patthy L (2001) [11279007]
  Localization of disulfide bonds in the frizzled module of Ror1 receptor tyrosine kinase.
  J Biol Chem 276, 18485-90
20.   Liepinsh E, Trexler M, Kaikkonen A, Weigelt J, Bányai L, Patthy L and Otting G (2001) [11574466]
  NMR structure of the LCCL domain and implications for DFNA9 deafness disorder.
  EMBO J 20, 5347-53
21.   Ozhogina OA, Trexler M, Bányai L, Llinás M and Patthy L (2001) [11567102]
  Origin of fibronectin type II (FN2) modules: structural analyses of distantly-related members of the kringle family idey the kringle domain of neurotrypsin as a potential link between FN2 domains and kringles.
  Protein Sci 10, 2114-22
22.   Trexler M, Bányai L and Patthy L (2000) [10971586]
  The LCCL module.
  Eur J Biochem 267, 5751-7
23.   Zhao Z, Jin L, Fu YX, Ramsay M, Jenkins T, Leskinen E, Pamilo P, Trexler M, Patthy L, Jorde LB, Ramos-Onsins S, Yu N and Li WH (2000) [11005839]
  Worldwide DNA sequence variation in a 10-kilobase noncoding region on human chromosome 22.
  P Natl Acad Sci Usa 97, 11354-8
24.   Constantine KL, Madrid M, Bányai L, Trexler M, Patthy L and Llinás M (1992) [1731074]
  Refined solution structure and ligand-binding properties of PDC-109 domain b. A collagen-binding type II domain.
  J Mol Biol 223, 281-98
25.   Constantine KL, Ramesh V, Bányai L, Trexler M, Patthy L and Llinás M (1991) [1993183]
  Sequence-specific 1H NMR assignments and structural characterization of bovine seminal fluid protein PDC-109 domain b.
  Biochemistry-us 30, 1663-72
26.   Bányai L, Trexler M, Koncz S, Gyenes M, Sipos G and Patthy L (1990) [2249694]
  The collagen-binding site of type-II units of bovine seminal fluid protein PDC-109 and fibronectin.
  Eur J Biochem 193, 801-6
27.   De Marco A, Pluck ND, Bányai L, Trexler M, Laursen RA, Patthy L, Llinás M and Williams RJ (1985) [3994983]
  Analysis and identification of aromatic signals in the proton magnetic resonance spectrum of the kringle 4 fragment from human plasminogen.
  Biochemistry-us 24, 748-53
28.   Trexler M, Bányai L, Patthy L, Pluck ND and Williams RJ (1985) [2996892]
  Chemical modification and nuclear magnetic resonance studies on human plasminogen kringle 4. Assignment of tyrosine and histidine resonances to specific residues in the sequence.
  Eur J Biochem 152, 439-46
29.   Patthy L, Trexler M, Váli Z, Bányai L and Váradi A (1984) [6373375]
  Kringles: modules specialized for protein binding. Homology of the gelatin-binding region of fibronectin with the kringle structures of proteases.
  FEBS Lett 171, 131-6
30.   Trexler M and Patthy L (1984) [6329306]
  Residues Cys-1 and Cys-79 are not essential for refolding of reduced-denatured kringle 4 fragment of human plasminogen.
  Biochim Biophys Acta 787, 275-80
31.   Trexler M and Patthy L (1983) [6302685]
  Folding autonomy of the kringle 4 fragment of human plasminogen.
  P Natl Acad Sci Usa 80, 2457-61
32.   Trexler M, Banyai L, Patthy L, Pluck ND and Williams RJP (1983) [-100002735]
  The solution structure of kringle 4. NMR studies on native and several chemically modified kringle 4 species of human plasminogen.
  FEBS Lett 154, 311-318
33.   Trexler M, Váli Z and Patthy L (1982) [6919539]
  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.
  J Biol Chem 257, 7401-6

Books or book chapters

1.   Patthy L, Trexler M, Váli Z, Bányai L and Váradi A (1984)
  Kringle structures of human plasminogen: their role in the regulation of fibrinolysis.
  Symp.Biol.Hung. 25, 73-79