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Maria Trexler
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Publications
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