János Mótyán

Name:         János András Mótyán
Nationality:  Hungarian
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Assistant lecturer
Department of Biochemistry and Molecular Biology
Facutly of Medicine
University of Debrecen,Laboratory of Retroviral Biochemistry

Office address:

Department of Biochemistry and Molecular Biology,
Research Center for Molecular Medicine,
University of Debrecen
Life Science Building, Egyetem tér 1., Debrecen, Hungary H-4010

Location:

Life Science Building; 3.109 office
Phone: (+36 52) 411-600/65858
(+36 52) 416-432
Fax: +36-52-314989

Studies on retroviral and retroviral like aspartic proteases

- PEG10 (Paternally expressed gene 10) protease
- SASPase (skin-specific aspartic protease) protease
- MSRV (multiple-sclerosis associated retrovirus) protease

Studies on human NOD-like receptor family CARD domain containing 5 (NLRC5) protein

- comparative studies of substrate specificities
- in silico: structural bioinformatical studies (sequence alignments, homology modeling)
- in vitro: molecular biological and biochemical studies on the proteins

Publications:

2013

Research Applications of Proteolytic Enzymes in Molecular Biology (review)
Mótyán J.A., Tóth F., Tőzsér J.
Biomolecules 3 (2013) 923-942.

A molecular model of the full-length human NOD-like receptor family CARD domain containing 5 (NLRC5) protein 
Mótyán J.A., Bagossi P., Benkő S., Tőzsér J. 
BMC Bioinformatics (2013) 14 (1): 275.

2012

Inhibition of XMRV and HIV-1 proteases by pepstatin A and acetyl-pepstatin
K Matúz, J Mótyán, M Li, A Wlodawer, J Tőzsér
FEBS J. 279 (17): 3276-86.

The digestable parent cyclodextrin
J Harangi, G Béke, M Harangi, JA Mótyán
Journal of Inclusion Phenomena and Macrocyclic Chemistry 73:335–339

2011

Transglycosylation by barley α-amylase 1
JA Mótyán, E Fazekas, H Mori, B Svensson, P Bagossi, L Kandra, G Gyémánt
Journal of Molecular Catalysis B: Enzymatic 72 (3), 229-237

Computer-aided subsite mapping of α-amylases
JA Mótyán, G Gyémánt, J Harangi, P Bagossi
Carbohydrate Research 346 (3), 410-415

2010
New Insight into Structure/Function Relationships in Plant. ALPHA.-Amylase Family GH13 Members
Seo, E.S. Andersen, J. M., Nielsen, M. M., Vester-Christensen, M. B., Christiansen, C., Jensen, J.M., Mótyán, J. A.,Glaring, M. A., Blennow, A., Kandra, L., Gyémánt, G., Janeček, Š., Haser, R., Aghajari, N., Hachem, M. A., Svensson, B.Journal of Applied Glycoscience 57 (2), 157-162

2009
Two secondary carbohydrate binding sites on the surface of barley α-amylase 1 have distinct functions and display synergy in hydrolysis of starch granules
Nielsen M. M., Bozonnet S., Seo E. S., Mótyán J. A., Andersen J. M., Dilokpimol A., Abou Hachem M., Gyémánt G., Næsted H., Kandra L., Sigurskjold B. W., Svensson B.
Biochemistry 48 (32), 7686-7697

Debrecen, 2014.09.05.