TY  - DATA
AU  - Mihailović-Vesić, Jelena
AU  - Inić-Kanada, Aleksandra
AU  - Smiljanić, Katarina
AU  - Stein, Elisabeth
AU  - Barisani-Asenbauer, T.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3563
T2  - EuPA Open Proteomics
T1  - Supplementary data for the article: Mihailovic, J.; Inic-Kanada, A.; Smiljanic, K.; Stein, E.; Barisani-Asenbauer, T.; Cirkovic Velickovic, T. Lysine Acetylation of Major Chlamydia Trachomatis Antigens. EuPA Open Proteomics 2016, 10, 63–69. https://doi.org/10.1016/j.euprot.2016.01.007
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3563
ER  - 

@misc{
author = "Mihailović-Vesić, Jelena and Inić-Kanada, Aleksandra and Smiljanić, Katarina and Stein, Elisabeth and Barisani-Asenbauer, T. and Ćirković-Veličković, Tanja",
year = "2016",
journal = "EuPA Open Proteomics",
title = "Supplementary data for the article: Mihailovic, J.; Inic-Kanada, A.; Smiljanic, K.; Stein, E.; Barisani-Asenbauer, T.; Cirkovic Velickovic, T. Lysine Acetylation of Major Chlamydia Trachomatis Antigens. EuPA Open Proteomics 2016, 10, 63–69. https://doi.org/10.1016/j.euprot.2016.01.007",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3563"
}

Mihailović-Vesić, J., Inić-Kanada, A., Smiljanić, K., Stein, E., Barisani-Asenbauer, T.,& Ćirković-Veličković, T.. (2016). Supplementary data for the article: Mihailovic, J.; Inic-Kanada, A.; Smiljanic, K.; Stein, E.; Barisani-Asenbauer, T.; Cirkovic Velickovic, T. Lysine Acetylation of Major Chlamydia Trachomatis Antigens. EuPA Open Proteomics 2016, 10, 63–69. https://doi.org/10.1016/j.euprot.2016.01.007. in EuPA Open Proteomics.
https://hdl.handle.net/21.15107/rcub_cherry_3563

Mihailović-Vesić J, Inić-Kanada A, Smiljanić K, Stein E, Barisani-Asenbauer T, Ćirković-Veličković T. Supplementary data for the article: Mihailovic, J.; Inic-Kanada, A.; Smiljanic, K.; Stein, E.; Barisani-Asenbauer, T.; Cirkovic Velickovic, T. Lysine Acetylation of Major Chlamydia Trachomatis Antigens. EuPA Open Proteomics 2016, 10, 63–69. https://doi.org/10.1016/j.euprot.2016.01.007. in EuPA Open Proteomics. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3563 .

Mihailović-Vesić, Jelena, Inić-Kanada, Aleksandra, Smiljanić, Katarina, Stein, Elisabeth, Barisani-Asenbauer, T., Ćirković-Veličković, Tanja, "Supplementary data for the article: Mihailovic, J.; Inic-Kanada, A.; Smiljanic, K.; Stein, E.; Barisani-Asenbauer, T.; Cirkovic Velickovic, T. Lysine Acetylation of Major Chlamydia Trachomatis Antigens. EuPA Open Proteomics 2016, 10, 63–69. https://doi.org/10.1016/j.euprot.2016.01.007" in EuPA Open Proteomics (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3563 .

TY  - JOUR
AU  - Mihailović-Vesić, Jelena
AU  - Inić-Kanada, Aleksandra
AU  - Smiljanić, Katarina
AU  - Stein, Elisabeth
AU  - Barisani-Asenbauer, T.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/295
AB  - Chlamydia trachomatis (Ct) is a human pathogen causing trachoma and infertility. We investigated acetylation at lysine residues of chlamydial antigenic proteins: major outer membrane protein (MOMP), 60 kDa chaperonin (chlamydial Hsp60), elongation factor G (EF-G), enolase and the polymorphic membrane proteins PmpB, PmpE and PmpF. 60 kDa chaperonin, EF-G and PmpB showed the highest degree of acetylation. Our data show that important Ct antigens could be post-translationally modified by acetylation of lysine residues at multiple sites. Further studies are needed to investigate total acetylome of Ct and the impact PTMs might have on Ct biology and pathogenicity. © 2016.
T2  - EuPA Open Proteomics
T1  - Lysine acetylation of major Chlamydia trachomatis antigens
VL  - 10
SP  - 63
EP  - 69
DO  - 10.1016/j.euprot.2016.01.007
ER  - 

@article{
author = "Mihailović-Vesić, Jelena and Inić-Kanada, Aleksandra and Smiljanić, Katarina and Stein, Elisabeth and Barisani-Asenbauer, T. and Ćirković-Veličković, Tanja",
year = "2016",
abstract = "Chlamydia trachomatis (Ct) is a human pathogen causing trachoma and infertility. We investigated acetylation at lysine residues of chlamydial antigenic proteins: major outer membrane protein (MOMP), 60 kDa chaperonin (chlamydial Hsp60), elongation factor G (EF-G), enolase and the polymorphic membrane proteins PmpB, PmpE and PmpF. 60 kDa chaperonin, EF-G and PmpB showed the highest degree of acetylation. Our data show that important Ct antigens could be post-translationally modified by acetylation of lysine residues at multiple sites. Further studies are needed to investigate total acetylome of Ct and the impact PTMs might have on Ct biology and pathogenicity. © 2016.",
journal = "EuPA Open Proteomics",
title = "Lysine acetylation of major Chlamydia trachomatis antigens",
volume = "10",
pages = "63-69",
doi = "10.1016/j.euprot.2016.01.007"
}

Mihailović-Vesić, J., Inić-Kanada, A., Smiljanić, K., Stein, E., Barisani-Asenbauer, T.,& Ćirković-Veličković, T.. (2016). Lysine acetylation of major Chlamydia trachomatis antigens. in EuPA Open Proteomics, 10, 63-69.
https://doi.org/10.1016/j.euprot.2016.01.007

Mihailović-Vesić J, Inić-Kanada A, Smiljanić K, Stein E, Barisani-Asenbauer T, Ćirković-Veličković T. Lysine acetylation of major Chlamydia trachomatis antigens. in EuPA Open Proteomics. 2016;10:63-69.
doi:10.1016/j.euprot.2016.01.007 .

Mihailović-Vesić, Jelena, Inić-Kanada, Aleksandra, Smiljanić, Katarina, Stein, Elisabeth, Barisani-Asenbauer, T., Ćirković-Veličković, Tanja, "Lysine acetylation of major Chlamydia trachomatis antigens" in EuPA Open Proteomics, 10 (2016):63-69,
https://doi.org/10.1016/j.euprot.2016.01.007 . .