TY  - PAT
AU  - Andjelković, Uroš
AU  - Sladić, Dušan
AU  - Vukasinović, Ivana
AU  - Lah, Jurij
AU  - Fonovic, Marko
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6941
AB  - The present invention relates to a novel polypeptide which displays specific carbohydrate binding activity, particularly against glycans that contain mannose, and in vivo and ex vivo methods of use thereof. Methods of use comprise administering a polypeptide of the invention, for example to a sample or a subject in which carbohydrate is present, under conditions suitable for the polypeptide to bind the carbohydrate. The carbohydrate may be expressed by a pathogen. The invention relates to polypeptides and compositions thereof with anti-pathogen activity, such as anti-viral, anti-bacterial, anti-fungal or anti-tumour activity. Also provided are methods for the prevention or treatment of diseases and conditions mediated by pathogens which express carbohydrate, for example as glycoproteins.
PB  - The World Intellectual Property Organization
T2  - The World Intellectual Property Organization
T1  - Carbohydrate binding polypeptide of Savalia Savaglia
IS  - WO20230552505A1
UR  - https://hdl.handle.net/21.15107/rcub_cer_6941
ER  - 

@misc{
author = "Andjelković, Uroš and Sladić, Dušan and Vukasinović, Ivana and Lah, Jurij and Fonovic, Marko",
year = "2023",
abstract = "The present invention relates to a novel polypeptide which displays specific carbohydrate binding activity, particularly against glycans that contain mannose, and in vivo and ex vivo methods of use thereof. Methods of use comprise administering a polypeptide of the invention, for example to a sample or a subject in which carbohydrate is present, under conditions suitable for the polypeptide to bind the carbohydrate. The carbohydrate may be expressed by a pathogen. The invention relates to polypeptides and compositions thereof with anti-pathogen activity, such as anti-viral, anti-bacterial, anti-fungal or anti-tumour activity. Also provided are methods for the prevention or treatment of diseases and conditions mediated by pathogens which express carbohydrate, for example as glycoproteins.",
publisher = "The World Intellectual Property Organization",
journal = "The World Intellectual Property Organization",
title = "Carbohydrate binding polypeptide of Savalia Savaglia",
number = "WO20230552505A1",
url = "https://hdl.handle.net/21.15107/rcub_cer_6941"
}

Andjelković, U., Sladić, D., Vukasinović, I., Lah, J.,& Fonovic, M.. (2023). Carbohydrate binding polypeptide of Savalia Savaglia. in The World Intellectual Property Organization
The World Intellectual Property Organization.(WO20230552505A1).
https://hdl.handle.net/21.15107/rcub_cer_6941

Andjelković U, Sladić D, Vukasinović I, Lah J, Fonovic M. Carbohydrate binding polypeptide of Savalia Savaglia. in The World Intellectual Property Organization. 2023;(WO20230552505A1).
https://hdl.handle.net/21.15107/rcub_cer_6941 .

Andjelković, Uroš, Sladić, Dušan, Vukasinović, Ivana, Lah, Jurij, Fonovic, Marko, "Carbohydrate binding polypeptide of Savalia Savaglia" in The World Intellectual Property Organization, no. WO20230552505A1 (2023),
https://hdl.handle.net/21.15107/rcub_cer_6941 .

TY  - CONF
AU  - Anđelković, Uroš
AU  - Pajic, I.
AU  - Vizovisek, M.
AU  - Vidmar, R.
AU  - Prislan, I.
AU  - Tufegdžić, Srđan
AU  - Fonovic, M.
AU  - Lah, Jurij
AU  - Turk, B.
AU  - Sladić, Dušan
PY  - 2013
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1302
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal
T1  - A new lectin from coral Gerardia savaglia: purification, physico-chemical characterization and thermodynamics of saccharide binding
VL  - 280 (Supp. 1)
SP  - 531
EP  - 531
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1419
ER  - 

@conference{
author = "Anđelković, Uroš and Pajic, I. and Vizovisek, M. and Vidmar, R. and Prislan, I. and Tufegdžić, Srđan and Fonovic, M. and Lah, Jurij and Turk, B. and Sladić, Dušan",
year = "2013",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal",
title = "A new lectin from coral Gerardia savaglia: purification, physico-chemical characterization and thermodynamics of saccharide binding",
volume = "280 (Supp. 1)",
pages = "531-531",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1419"
}

Anđelković, U., Pajic, I., Vizovisek, M., Vidmar, R., Prislan, I., Tufegdžić, S., Fonovic, M., Lah, J., Turk, B.,& Sladić, D.. (2013). A new lectin from coral Gerardia savaglia: purification, physico-chemical characterization and thermodynamics of saccharide binding. in FEBS Journal
Wiley-Blackwell, Hoboken., 280 (Supp. 1), 531-531.
https://hdl.handle.net/21.15107/rcub_cherry_1419

Anđelković U, Pajic I, Vizovisek M, Vidmar R, Prislan I, Tufegdžić S, Fonovic M, Lah J, Turk B, Sladić D. A new lectin from coral Gerardia savaglia: purification, physico-chemical characterization and thermodynamics of saccharide binding. in FEBS Journal. 2013;280 (Supp. 1):531-531.
https://hdl.handle.net/21.15107/rcub_cherry_1419 .

Anđelković, Uroš, Pajic, I., Vizovisek, M., Vidmar, R., Prislan, I., Tufegdžić, Srđan, Fonovic, M., Lah, Jurij, Turk, B., Sladić, Dušan, "A new lectin from coral Gerardia savaglia: purification, physico-chemical characterization and thermodynamics of saccharide binding" in FEBS Journal, 280 (Supp. 1) (2013):531-531,
https://hdl.handle.net/21.15107/rcub_cherry_1419 .

TY  - JOUR
AU  - Mernik, Andrej
AU  - Anđelković, Uroš
AU  - Drobnak, Igor
AU  - Lah, Jurij
PY  - 2012
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1091
AB  - Ccd system is a toxin-antitoxin module (operon) located on plasmids and chromosomes of bacteria. CcdB(F) encoded by ccd operon located on Escherichia coli plasmid F and CcdB(Vfi) encoded by ccd operon located on Vibrio fischeri chromosome are members of the CcdB family of toxins. Native CcdBs are dimers that bind to gyrase-DNA complexes and inhibit DNA transcription and replication. While thermodynamic stability and unfolding characteristics of the plasmidic CcdB(F) in denaturant solutions are reported in detail, the corresponding information on the chromosomal CcdB(Vfi) is rather scarce. Therefore, we studied urea-induced unfolding of CcdB(Vfi) at various temperatures and protein concentrations by circular dichroism spectroscopy. Global model analysis of spectroscopic data suggests that CcdB(Vfi) dimer unfolds to the corresponding monomeric components in a reversible two-state manner. Results reveal that at physiological temperatures CcdB(Vfi) exhibits lower thermodynamic stability compared to CcdB(F). At high urea concentrations CcdB(Vfi), similarly to CcdB(F), retains a significant amount of secondary structure. Differences in thermodynamic parameters of CcdB(Vfi) and CcdB(F) unfolding can reasonably be explained by the differences in their structural features.
PB  - Slovenian Chemical Society
T2  - Acta Chimica Slovenica
T1  - Differences in Unfolding Energetics of CcdB Toxins From V. fischeri and E. coli
VL  - 59
IS  - 3
SP  - 548
EP  - 553
UR  - https://hdl.handle.net/21.15107/rcub_cer_1091
ER  - 

@article{
author = "Mernik, Andrej and Anđelković, Uroš and Drobnak, Igor and Lah, Jurij",
year = "2012",
abstract = "Ccd system is a toxin-antitoxin module (operon) located on plasmids and chromosomes of bacteria. CcdB(F) encoded by ccd operon located on Escherichia coli plasmid F and CcdB(Vfi) encoded by ccd operon located on Vibrio fischeri chromosome are members of the CcdB family of toxins. Native CcdBs are dimers that bind to gyrase-DNA complexes and inhibit DNA transcription and replication. While thermodynamic stability and unfolding characteristics of the plasmidic CcdB(F) in denaturant solutions are reported in detail, the corresponding information on the chromosomal CcdB(Vfi) is rather scarce. Therefore, we studied urea-induced unfolding of CcdB(Vfi) at various temperatures and protein concentrations by circular dichroism spectroscopy. Global model analysis of spectroscopic data suggests that CcdB(Vfi) dimer unfolds to the corresponding monomeric components in a reversible two-state manner. Results reveal that at physiological temperatures CcdB(Vfi) exhibits lower thermodynamic stability compared to CcdB(F). At high urea concentrations CcdB(Vfi), similarly to CcdB(F), retains a significant amount of secondary structure. Differences in thermodynamic parameters of CcdB(Vfi) and CcdB(F) unfolding can reasonably be explained by the differences in their structural features.",
publisher = "Slovenian Chemical Society",
journal = "Acta Chimica Slovenica",
title = "Differences in Unfolding Energetics of CcdB Toxins From V. fischeri and E. coli",
volume = "59",
number = "3",
pages = "548-553",
url = "https://hdl.handle.net/21.15107/rcub_cer_1091"
}

Mernik, A., Anđelković, U., Drobnak, I.,& Lah, J.. (2012). Differences in Unfolding Energetics of CcdB Toxins From V. fischeri and E. coli. in Acta Chimica Slovenica
Slovenian Chemical Society., 59(3), 548-553.
https://hdl.handle.net/21.15107/rcub_cer_1091

Mernik A, Anđelković U, Drobnak I, Lah J. Differences in Unfolding Energetics of CcdB Toxins From V. fischeri and E. coli. in Acta Chimica Slovenica. 2012;59(3):548-553.
https://hdl.handle.net/21.15107/rcub_cer_1091 .

Mernik, Andrej, Anđelković, Uroš, Drobnak, Igor, Lah, Jurij, "Differences in Unfolding Energetics of CcdB Toxins From V. fischeri and E. coli" in Acta Chimica Slovenica, 59, no. 3 (2012):548-553,
https://hdl.handle.net/21.15107/rcub_cer_1091 .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Lah, Jurij
PY  - 2011
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/923
AB  - Recently, four external invertase isoforms (EINV1, EINV2, EINV3, and EINV4) have been isolated from S. cerevisiae. However, there is nothing known about their structural features and thermodynamics of unfolding. Since this information is essential for understanding their functioning at the molecular level as well as applicable in the food industry, we investigated guanidinium-chloride induced structural changes of the isoforms by CD and fluorescence spectroscopy. The resulting unfolding curves measured for each isoform at different temperatures were described simultaneously by a reversible two-state model to obtain the corresponding thermodynamic parameters. Here, we show that they are different for different isoforms and demonstrate that they correlate with the surface charge density of the native isoforms which follows the order EINV1  LT  EINV2  LT  EINV3  LT  EINV4. It appears that at physiological temperatures the thermodynamic stability of the isoforms follows the same order, while above 55 degrees C, the order is the opposite EINV1 > EINV2 > EINV3 approximate to EINV4. This suggests that increasing the efficiency of the food industry processes involving inverta,se would require the application of EINV3 and/or EINV4 at physiological temperatures and EINV1 at elevated temperatures.
PB  - American Chemical Society (ACS)
T2  - Journal of Agricultural and Food Chemistry
T1  - Thermodynamics and Structural Features of the Yeast Saccharomyces cerevisiae External Invertase Isoforms in Guanidinium-chloride Solutions
VL  - 59
IS  - 2
SP  - 727
EP  - 732
DO  - 10.1021/jf103441p
ER  - 

@article{
author = "Anđelković, Uroš and Lah, Jurij",
year = "2011",
abstract = "Recently, four external invertase isoforms (EINV1, EINV2, EINV3, and EINV4) have been isolated from S. cerevisiae. However, there is nothing known about their structural features and thermodynamics of unfolding. Since this information is essential for understanding their functioning at the molecular level as well as applicable in the food industry, we investigated guanidinium-chloride induced structural changes of the isoforms by CD and fluorescence spectroscopy. The resulting unfolding curves measured for each isoform at different temperatures were described simultaneously by a reversible two-state model to obtain the corresponding thermodynamic parameters. Here, we show that they are different for different isoforms and demonstrate that they correlate with the surface charge density of the native isoforms which follows the order EINV1  LT  EINV2  LT  EINV3  LT  EINV4. It appears that at physiological temperatures the thermodynamic stability of the isoforms follows the same order, while above 55 degrees C, the order is the opposite EINV1 > EINV2 > EINV3 approximate to EINV4. This suggests that increasing the efficiency of the food industry processes involving inverta,se would require the application of EINV3 and/or EINV4 at physiological temperatures and EINV1 at elevated temperatures.",
publisher = "American Chemical Society (ACS)",
journal = "Journal of Agricultural and Food Chemistry",
title = "Thermodynamics and Structural Features of the Yeast Saccharomyces cerevisiae External Invertase Isoforms in Guanidinium-chloride Solutions",
volume = "59",
number = "2",
pages = "727-732",
doi = "10.1021/jf103441p"
}

Anđelković, U.,& Lah, J.. (2011). Thermodynamics and Structural Features of the Yeast Saccharomyces cerevisiae External Invertase Isoforms in Guanidinium-chloride Solutions. in Journal of Agricultural and Food Chemistry
American Chemical Society (ACS)., 59(2), 727-732.
https://doi.org/10.1021/jf103441p

Anđelković U, Lah J. Thermodynamics and Structural Features of the Yeast Saccharomyces cerevisiae External Invertase Isoforms in Guanidinium-chloride Solutions. in Journal of Agricultural and Food Chemistry. 2011;59(2):727-732.
doi:10.1021/jf103441p .

Anđelković, Uroš, Lah, Jurij, "Thermodynamics and Structural Features of the Yeast Saccharomyces cerevisiae External Invertase Isoforms in Guanidinium-chloride Solutions" in Journal of Agricultural and Food Chemistry, 59, no. 2 (2011):727-732,
https://doi.org/10.1021/jf103441p . .