Miltner, N., Kalló, G., Csősz, É., Miczi, M., Nagy, T., Mahdi, M., Mótyán, J., Tőzsér, J.: Identification of SARS-CoV-2 Main Protease (Mpro) Cleavage Sites Using Two-Dimensional Electrophoresis and In Silico Cleavage Site Prediction.
Int. J. Mol. Sci. 24 (4), 1-19, 2023.

Chang Chien, Y., Madarász, K., Csoma, S., Mótyán, J., Huang, H., Méhes, G., Mokánszki, A.: Molecular Identification and In Silico Protein Analysis of a Novel BCOR-CLGN Gene Fusion in Intrathoracic BCOR-Rearranged Sarcoma.
Cancers (Basel). 15 (3), 1-17, 2023.

Hoffka, G., Lountos, G., Needle, D., Wlodawer, A., Waugh, D., Tőzsér, J., Mótyán, J.: Self-inhibited state of Venezuelan equine encephalitis virus (VEEV) nsP2 cysteine protease: a crystallographic and molecular dynamics analysis.
J. Mol. Biol. [Epub ahead of print] 1-50, 2023.

Madarász, K., Mótyán, J., Bedekovics, J., Miltényi, Z., Ujfalusi, A., Méhes, G., Mokánszki, A.: Deep Molecular and In Silico Protein Analysis of p53 Alteration in Myelodysplastic Neoplasia and Acute Myeloid Leukemia.
Cells. 11 (21), 1-23, 2022.

Mótyán, J., Kassay, N., Matúz, K., Tőzsér, J.: Different Mutation Tolerance of Lentiviral (HIV-1) and Deltaretroviral (BLV and HTLV) Protease Precursors.
Viruses-Basel. 14 (9), 1-17, 2022.

Miltner, N., Linkner, T., Ambrus, V., Al-Muffti, A., Ahmad, H., Mótyán, J., Benkő, S., Tőzsér, J., Mahdi, M.: Early suppression of antiviral host response and protocadherins by SARS-CoV-2 Spike protein in THP-1-derived macrophage-like cells.
Front. Immunol. 13 999233, 2022.

Mótyán, J., Mahdi, M., Hoffka, G., Tőzsér, J.: Potential Resistance of SARS-CoV-2 Main Protease (Mpro) against Protease Inhibitors: lessons Learned from HIV-1 Protease.
Int. J. Mol. Sci. 23 (7), 1-20, 2022.

Kassay, N., Mótyán, J., Matúz, K., Golda, M., Tőzsér, J.: Biochemical Characterization, Specificity and Inhibition Studies of HTLV-1, HTLV-2, and HTLV-3 Proteases.
Life (Basel). 11 (2), 1-21, 2021.

Miczi, M., Diós, Á., Bozóki, B., Tőzsér, J., Mótyán, J.: Development of a Bio-Layer Interferometry-Based Protease Assay Using HIV-1 Protease as a Model.
Viruses-Basel. 13 (6), 1-20, 2021.

Mokánszki, A., Chang Chien, Y., Mótyán, J., Juhász, P., Bádon, E., Madar, L., Szegedi, I., Kiss, C., Méhes, G.: Novel RB1 and MET Gene Mutations in a Case with Bilateral Retinoblastoma Followed by Multiple Metastatic Osteosarcoma.
Diagnostics. 11 (1), 1-11, 2021.

Mótyán, J., Miczi, M., Oroszlan, S., Tőzsér, J.: Specificity of the HIV-1 Protease on Substrates Representing the Cleavage Site in the Proximal Zinc-Finger of HIV-1 Nucleocapsid Protein.
Viruses-Basel. 13 (6), 1-14, 2021.

Mahdi, M., Mótyán, J., Szojka, Z., Golda, M., Miczi, M., Tőzsér, J.: Analysis of the efficacy of HIV protease inhibitors against SARS-CoV-2·s main protease.
Virol. J. 17 (1), 1-8, 2020.

Golda, M., Mótyán, J., Nagy, K., Matúz, K., Nagy, T., Tőzsér, J.: Biochemical characterization of human retroviral-like aspartic protease 1 (ASPRV1).
Biomolecules. 10 (7), 1-25, 2020.

Gazda, L., Matúz, K., Nagy, T., Mótyán, J., Tőzsér, J.: Biochemical characterization of Ty1 retrotransposon protease.
PLoS One. 15 (1), 1-24, 2020.

Mótyán, J., Miczi, M., Tőzsér, J.: Dimer Interface Organization is a Main Determinant of Intermonomeric Interactions and Correlates with Evolutionary Relationships of Retroviral and Retroviral-Like Ddi1 and Ddi2 Proteases.
Int. J. Mol. Sci. 21 (4), 1-24, 2020.

Golda, M., Mótyán, J., Mahdi, M., Tőzsér, J.: Functional Study of the Retrotransposon-Derived Human PEG10 Protease.
Int. J. Mol. Sci. 21 (7), 1-22, 2020.

Miczi, M., Golda, M., Kunkli, B., Nagy, T., Tőzsér, J., Mótyán, J.: Identification of Host Cellular Protein Substrates of SARS-COV-2 Main Protease.
Int. J. Mol. Sci. 21 (24), 1-19, 2020.

Bozóki, B., Mótyán, J., Hoffka, G., Waugh, D., Tőzsér, J.: Specificity Studies of the Venezuelan Equine Encephalitis Virus Non-Structural Protein 2 Protease Using Recombinant Fluorescent Substrates.
Int. J. Mol. Sci. 21 (20), 1-26, 2020.

Golda, M., Mótyán, J., Mahdi, M., Tőzsér, J.: Study of the Retrotransposon-Derived Human PEG10 Protease.
Proceedings. 50 (1), 110, 2020.

Szojka, Z., Mótyán, J., Miczi, M., Mahdi, M., Tőzsér, J.: Y44A Mutation in the Acidic Domain of HIV-2 Tat Impairs Viral Reverse Transcription and LTR-Transactivation.
Int. J. Mol. Sci. 21 (16), 1-17, 2020.

Diszházi, G., Magyar, Z., Mótyán, J., Csernoch, L., Jóna, I., Nánási, P., Almássy, J.: Dantrolene Requires Mg2+ and ATP To Inhibit the Ryanodine Receptor.
Mol. Pharmacol. 96 (3), 401-407, 2019.

Bozóki, B., Mótyán, J., Miczi, M., Gazda, L., Tőzsér, J.: Use of Recombinant Fusion Proteins in a Fluorescent Protease Assay Platform and Their In-gel Renaturation.
JoVE. 143 1-15, 2019.

Koczok, K., Merő, G., P. Szabó, G., Madar, L., Gombos, É., Ajzner, É., Mótyán, J., Hortobágyi, T., Balogh, I.: A novel point mutation affecting Asn76 of dystrophin protein leads to dystrophinopathy.
Neuromusc. Disord. 28 (2), 129-136, 2018.

Bozóki, B., Gazda, L., Tóth, F., Miczi, M., Mótyán, J., Tőzsér, J.: A recombinant fusion protein-based, fluorescent protease assay for high throughput-compatible substrate screening.
Anal. Biochem. 540-541 52-63, 2018.

Mótyán, J., Miczi, M., Bozóki, B., Tőzsér, J.: Data supporting Ni-NTA magnetic bead-based fluorescent protease assay using recombinant fusion protein substrates.
Data in Brief. 18 203-208, 2018.

Mahdi, M., Szojka, Z., Mótyán, J., Tőzsér, J.: Inhibitory effects of HIV-2 Vpx on replication of HIV-1.
J. Virol. 92 (14), 1-46, 2018.

Mótyán, J., Müller, V., Tőzsér, J.: Vírus proteázok.
In: Ezerarcú fehérjék. Szerk.: Buday László, Nyitray László, Perczel András, Semmelweis Kiadó, Budapest, 895-907, 2018. ISBN: 9789633314586

Thangaraju, K., Király, R., Mótyán, J., Ambrus, V., Fuxreiter, M., Fésüs, L.: Computational analyses of the effect of novel amino acid clusters of human transglutaminase 2 on its structure and function.
Amino Acids. 49 605-614, 2017.

Thangaraju, K., Király, R., Demény, M., Mótyán, J., Fuxreiter, M., Fésüs, L.: Genomic variants reveal differential evolutionary constraints on human transglutaminases and point towards unrecognized significance of transglutaminase 2.
PLoS One. 12 (3), 1-24, 2017.

Tóth, F., Kádas, J., Mótyán, J., Tőzsér, J.: Effect of internal cleavage site mutations in human immunodeficiency virus type 1 capsid protein on its structure and function.
FEBS Open Bio. 6 (8), 847-859, 2016.

Mahdi, M., Szojka, Z., Mótyán, J., Tőzsér, J.: Inhibition Profiling of Retroviral Protease Inhibitors Using an HIV-2 Modular System.
Viruses. 7 (12), 6152-6162, 2015.

Mótyán, J., Bagossi, P., Benkő, S., Tőzsér, J.: A molecular model of the full-length human NOD-like receptor family CARD domain containing 5 (NLRC5) protein.
BMC Bioinformatics. 14 (1), 1-11, 2013.

Mótyán, J., Tóth, F., Tőzsér, J.: Research Applications of Proteolytic Enzymes in Molecular Biology.
Biomolecules. 3 (4), 923-942, 2013.

Matúz, K., Mótyán, J., Li, M., Wlodawer, A., Tőzsér, J.: Inhibition of XMRV and HIV-1 proteases by pepstatin A and acetyl-pepstatin.
FEBS J. 279 (17), 3276-3286, 2012.

Mótyán, J., Gyémánt, G., Harangi, J., Bagossi, P.: Computer-aided subsite mapping of alpha-amylases.
Carbohydr. Res. 346 (3), 410-415, 2011.

Harangi, J., Béke, G., Harangi, M., Mótyán, J.: The digestable parent cyclodextrin.
J. Incl. Phenom. Macrocycl. Chem. 73 (1-4), 335-339, 2011.

Mótyán, J., Fazekas, E., Mori, H., Svensson, B., Bagossi, P., Kandra, L., Gyémánt, G.: Transglycosylation by barley alfa-amylase 1.
J. Mol. Catal. B-Enzym. 72 (3-4), 229-237, 2011.

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

Nielsen, M., Bozonnet, S., Seo, E., Mótyán, J., Andersen, J., Dilokpimol, A., Abou Hachem, M., Gyémánt, G., Naested, H., Kandra, L., Sigurskjold, B., Svensson, B.: Two Secondary Carbohydrate Binding Sites on the Surface of Barley alpha-Amylase 1 Have Distinct Functions and Display Synergy in Hydrolysis of Starch Granules.
Biochemistry. 48 (32), 7686-7697, 2009.