TY  - CONF
AU  - Milić Komić, Sonja
AU  - Stevanović, Strahinja
AU  - Vidović, Marija
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4507
AB  - Ramonda serbica Panc. is a resurrection plant that can survive long desiccation periods (extreme loss of cellular water). The accumulation of late embryogenesis abundant proteins (LEAPs) is a crucial step in desiccation tolerance mechanism. Based on in vitro studies, LEAPs can be involved in antioxidative defense, ion sequestration, structural stabilization of both membranes and enzymes during freezing or drying, while by forming intracellular proteinaceous condensates they increase structural integrity and intracellular viscosity of cells during desiccation. Here we investigated the antioxidative potential of LEAPs identified by de novo transcriptomics of R. serbica, based on their primary and secondary confirmation. In our
previous work [1], we displayed the antioxidative capacity of 20 free proteogenic amino acids
(FAA) through determining their hydroxyl radical (•OH, generated in Fenton reaction) scavenging
rate by using electron paramagnetic resonance. These results served as a basis for generating a model for prediction of •OH scavenging activity for selected proteins. In addition, the model was built based on protein primary sequences, hydrophobicity, 3D structure and predicted solvent accessible area. Manually curated data for peptides and proteins with experimentally determined •OH scavenging rate were used for training and testing. The model was fed into machine learning algorithm and •OH scavenging potential scale was created using IC50 values. By applying our model, we classified 164 LEAPs according to their potential for •OH scavenging. Further work will focus on the experimental evaluation of the obtained model by measuring of the rate of • OH scavenging in the presence of recombinantly produced LEAPs.
C3  - Annual Meeting, SFRR-E 2021 Belgrade, Serbia, 15-18 June
T1  - Hydroxyl radical scavenging potential of the late embryogenesis abundant proteins (LEA) proteins from Ramonda serbica – in silico approach
SP  - 214
EP  - 214
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4507
ER  - 

@conference{
author = "Milić Komić, Sonja and Stevanović, Strahinja and Vidović, Marija",
year = "2021",
abstract = "Ramonda serbica Panc. is a resurrection plant that can survive long desiccation periods (extreme loss of cellular water). The accumulation of late embryogenesis abundant proteins (LEAPs) is a crucial step in desiccation tolerance mechanism. Based on in vitro studies, LEAPs can be involved in antioxidative defense, ion sequestration, structural stabilization of both membranes and enzymes during freezing or drying, while by forming intracellular proteinaceous condensates they increase structural integrity and intracellular viscosity of cells during desiccation. Here we investigated the antioxidative potential of LEAPs identified by de novo transcriptomics of R. serbica, based on their primary and secondary confirmation. In our
previous work [1], we displayed the antioxidative capacity of 20 free proteogenic amino acids
(FAA) through determining their hydroxyl radical (•OH, generated in Fenton reaction) scavenging
rate by using electron paramagnetic resonance. These results served as a basis for generating a model for prediction of •OH scavenging activity for selected proteins. In addition, the model was built based on protein primary sequences, hydrophobicity, 3D structure and predicted solvent accessible area. Manually curated data for peptides and proteins with experimentally determined •OH scavenging rate were used for training and testing. The model was fed into machine learning algorithm and •OH scavenging potential scale was created using IC50 values. By applying our model, we classified 164 LEAPs according to their potential for •OH scavenging. Further work will focus on the experimental evaluation of the obtained model by measuring of the rate of • OH scavenging in the presence of recombinantly produced LEAPs.",
journal = "Annual Meeting, SFRR-E 2021 Belgrade, Serbia, 15-18 June",
title = "Hydroxyl radical scavenging potential of the late embryogenesis abundant proteins (LEA) proteins from Ramonda serbica – in silico approach",
pages = "214-214",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4507"
}

Milić Komić, S., Stevanović, S.,& Vidović, M.. (2021). Hydroxyl radical scavenging potential of the late embryogenesis abundant proteins (LEA) proteins from Ramonda serbica – in silico approach. in Annual Meeting, SFRR-E 2021 Belgrade, Serbia, 15-18 June, 214-214.
https://hdl.handle.net/21.15107/rcub_cherry_4507

Milić Komić S, Stevanović S, Vidović M. Hydroxyl radical scavenging potential of the late embryogenesis abundant proteins (LEA) proteins from Ramonda serbica – in silico approach. in Annual Meeting, SFRR-E 2021 Belgrade, Serbia, 15-18 June. 2021;:214-214.
https://hdl.handle.net/21.15107/rcub_cherry_4507 .

Milić Komić, Sonja, Stevanović, Strahinja, Vidović, Marija, "Hydroxyl radical scavenging potential of the late embryogenesis abundant proteins (LEA) proteins from Ramonda serbica – in silico approach" in Annual Meeting, SFRR-E 2021 Belgrade, Serbia, 15-18 June (2021):214-214,
https://hdl.handle.net/21.15107/rcub_cherry_4507 .

TY  - CONF
AU  - Vidović, Marija
AU  - Stevanović, Strahinja
AU  - Pantelić, Ana
AU  - Veljović-Jovanović, Sonja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4510
AB  - Introduction: Ramonda serbica Panc. is a resurrection plant that can survive a long period of severe dehydrationdesiccation.
Desiccation induces cellular membrane integrity loss, protein aggregation, and denaturation, as well as
accelerated generation of reactive oxygen species. However, R. serbica can fully recover its metabolic functions
already one day upon watering [1].
Aim: to obtain more insight into the mechanisms of desiccation tolerance in R. serbica by differential de novo
transcriptomics of hydrated (HL) and desiccated leaves (DL).
C3  - Belgrade BioInformatics Conference 2021, 21-25 June, Vinča, Serbia
T1  - De Novo Transcriptome Sequencing of Ramonda serbica: Identification of the Candidate Genes Involved in the Desiccation Tolerance
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4510
ER  - 

@conference{
author = "Vidović, Marija and Stevanović, Strahinja and Pantelić, Ana and Veljović-Jovanović, Sonja",
year = "2021",
abstract = "Introduction: Ramonda serbica Panc. is a resurrection plant that can survive a long period of severe dehydrationdesiccation.
Desiccation induces cellular membrane integrity loss, protein aggregation, and denaturation, as well as
accelerated generation of reactive oxygen species. However, R. serbica can fully recover its metabolic functions
already one day upon watering [1].
Aim: to obtain more insight into the mechanisms of desiccation tolerance in R. serbica by differential de novo
transcriptomics of hydrated (HL) and desiccated leaves (DL).",
journal = "Belgrade BioInformatics Conference 2021, 21-25 June, Vinča, Serbia",
title = "De Novo Transcriptome Sequencing of Ramonda serbica: Identification of the Candidate Genes Involved in the Desiccation Tolerance",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4510"
}

Vidović, M., Stevanović, S., Pantelić, A.,& Veljović-Jovanović, S.. (2021). De Novo Transcriptome Sequencing of Ramonda serbica: Identification of the Candidate Genes Involved in the Desiccation Tolerance. in Belgrade BioInformatics Conference 2021, 21-25 June, Vinča, Serbia.
https://hdl.handle.net/21.15107/rcub_cherry_4510

Vidović M, Stevanović S, Pantelić A, Veljović-Jovanović S. De Novo Transcriptome Sequencing of Ramonda serbica: Identification of the Candidate Genes Involved in the Desiccation Tolerance. in Belgrade BioInformatics Conference 2021, 21-25 June, Vinča, Serbia. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4510 .

Vidović, Marija, Stevanović, Strahinja, Pantelić, Ana, Veljović-Jovanović, Sonja, "De Novo Transcriptome Sequencing of Ramonda serbica: Identification of the Candidate Genes Involved in the Desiccation Tolerance" in Belgrade BioInformatics Conference 2021, 21-25 June, Vinča, Serbia (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4510 .

TY  - CONF
AU  - Vidović, Marija
AU  - Stevanović, Strahinja
AU  - Franchin, Cinzia
AU  - Battisti, Ilaria
AU  - Arrigoni, Giorgio
AU  - Masi, Antonio
AU  - Veljović Jovanović, Sonja
PY  - 2021
UR  - https://inppo.org/inppo2020/
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4842
AB  - Resurrection plant Ramonda serbica Panc. survives desiccation for a long period and fully recovers metabolic functions already within one day upon watering [1]. Besides osmotic stress, desiccation provokes the accelerated generation of reactive oxygen species. The aim of our study was obtaining more insight into the mechanisms of desiccation tolerance in R. serbica by TMT labelled comparative quantitative proteomics of hydrated (HL) and desiccated leaves (DL). After de novo transcriptome analysis, 189456 transcripts with 189003 unigenes were annotated with seven common databases. Proteomic analysis allowed for the relative quantification of 895 different protein groups, 321 with a statistically significant difference in abundance between FL and DL. Among them, 25% referred to chloroplast and almost the same percentage were associated with desiccation and oxidative stress. Almost all differentially abundant proteins related to photosynthetic processes were down-regulated in DL, while those required for protein translation were more abundant in HL. Within differentially abundant proteins involved in antioxidative defence, the levels of enzymes involved in ascorbate-glutathione cycle, peroxiredoxins, Fe and Mn superoxide dismutase (SOD) were all reduced in DL, while germin-like proteins, three Cu/Zn SOD isoforms and polyphenol oxidases were more abundant in DL compared with HL. The protein family with the highest number of members showing the greatest accumulation upon desiccation comprised twenty different late embryogenesis abundant proteins (LEAPs), similarly as found by differential transcriptomic analysis. Taken together, our results imply a key role of LEAPs and Cu/Zn SOD in protective mechanism against desiccation in R. serbica, that may have significant implications on drought-related studies of crops grown in arid areas. This work was supported by the Science Fund of the Republic of Serbia (PROMIS project LEAPSyn-SCI, grant number 6039663). M.V. wishes to acknowledge the support of COST Action BM1405 for approving STSM in Padua during 2017 and 2018.
PB  - International Plant Proteomics Organization
C3  - The Fourth Conference of the International Plant Proteomics Organization
T1  - Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves
SP  - 43
EP  - 44
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4842
ER  - 

@conference{
author = "Vidović, Marija and Stevanović, Strahinja and Franchin, Cinzia and Battisti, Ilaria and Arrigoni, Giorgio and Masi, Antonio and Veljović Jovanović, Sonja",
year = "2021",
abstract = "Resurrection plant Ramonda serbica Panc. survives desiccation for a long period and fully recovers metabolic functions already within one day upon watering [1]. Besides osmotic stress, desiccation provokes the accelerated generation of reactive oxygen species. The aim of our study was obtaining more insight into the mechanisms of desiccation tolerance in R. serbica by TMT labelled comparative quantitative proteomics of hydrated (HL) and desiccated leaves (DL). After de novo transcriptome analysis, 189456 transcripts with 189003 unigenes were annotated with seven common databases. Proteomic analysis allowed for the relative quantification of 895 different protein groups, 321 with a statistically significant difference in abundance between FL and DL. Among them, 25% referred to chloroplast and almost the same percentage were associated with desiccation and oxidative stress. Almost all differentially abundant proteins related to photosynthetic processes were down-regulated in DL, while those required for protein translation were more abundant in HL. Within differentially abundant proteins involved in antioxidative defence, the levels of enzymes involved in ascorbate-glutathione cycle, peroxiredoxins, Fe and Mn superoxide dismutase (SOD) were all reduced in DL, while germin-like proteins, three Cu/Zn SOD isoforms and polyphenol oxidases were more abundant in DL compared with HL. The protein family with the highest number of members showing the greatest accumulation upon desiccation comprised twenty different late embryogenesis abundant proteins (LEAPs), similarly as found by differential transcriptomic analysis. Taken together, our results imply a key role of LEAPs and Cu/Zn SOD in protective mechanism against desiccation in R. serbica, that may have significant implications on drought-related studies of crops grown in arid areas. This work was supported by the Science Fund of the Republic of Serbia (PROMIS project LEAPSyn-SCI, grant number 6039663). M.V. wishes to acknowledge the support of COST Action BM1405 for approving STSM in Padua during 2017 and 2018.",
publisher = "International Plant Proteomics Organization",
journal = "The Fourth Conference of the International Plant Proteomics Organization",
title = "Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves",
pages = "43-44",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4842"
}

Vidović, M., Stevanović, S., Franchin, C., Battisti, I., Arrigoni, G., Masi, A.,& Veljović Jovanović, S.. (2021). Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves. in The Fourth Conference of the International Plant Proteomics Organization
International Plant Proteomics Organization., 43-44.
https://hdl.handle.net/21.15107/rcub_cherry_4842

Vidović M, Stevanović S, Franchin C, Battisti I, Arrigoni G, Masi A, Veljović Jovanović S. Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves. in The Fourth Conference of the International Plant Proteomics Organization. 2021;:43-44.
https://hdl.handle.net/21.15107/rcub_cherry_4842 .

Vidović, Marija, Stevanović, Strahinja, Franchin, Cinzia, Battisti, Ilaria, Arrigoni, Giorgio, Masi, Antonio, Veljović Jovanović, Sonja, "Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves" in The Fourth Conference of the International Plant Proteomics Organization (2021):43-44,
https://hdl.handle.net/21.15107/rcub_cherry_4842 .

TY  - CONF
AU  - Pantelić, Ana
AU  - Stevanović, Strahinja
AU  - Kilibarda, Nataša
AU  - Vidović, Marija
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4503
UR  - http://ojs.pmf.uns.ac.rs/index.php/dbe_serbica/index
AB  - An extreme loss of cellular water or desiccation (5-10% of relative water content) leads to protein denaturation, aggregation and degradation, and affects the fluidity of membrane lipids resulting in loss of membrane integrity [1]. The essential constituents of vegetative desiccation tolerance in so-called resurrection plants are late embryogenesis abundant proteins (LEAPs). This heterogeneous group of anhydrobiosis-related intrinsically disordered proteins forms mostly random conformation when fully hydrated, turning into compact α-helices during desiccation [2]. Based on in vitro studies, LEAPs can be involved in water binding, ion sequestration, stabilization of both membrane and enzymes during freezing or drying, while by forming intracellular proteinaceous condensates they increase structural integrity and intracellular viscosity of cells during desiccation.
Here, we identify 164 members of LEA gene family in endemic and relict resurrection species Ramonda serbica by integrating previously done de novo transcriptome and homologues protein motifs. Identified LEAPs were classification into six groups according to Protein family (PFAM) database and the most populated group was LEA4 containing 47% of total identified LEAPs. By using four secondary structure predictors, we showed that this group exhibited a high propensity to form amphipathic α-helices (81% of total sequence length is predicted to form α-helical structure). This implies that charged residues might be exposed to the solvent, while hydrophobic amino acids might interact with lipid bilayers or with other target proteins in the cell. In addition, as predicted by several bioinformatic tools, more than 70% of identified LEAPs were found to be highly disordered (~64%). Structural characterization of LEAPs is a key to understand their function and regulation of their intrinsic structural disorder-to-order transition during desiccation. These findings will promote transformative advancements in various fields, such as the development of new strategies in neurodegenerative disorders, cell preservation technology and the improvement of crop drought tolerance.
PB  - Novi Sad : Faculty of Sciences, Department of Biology and Ecology
C3  - Biologia Serbica
T1  - De Novo Transcriptome Sequencing of Ramonda serbica: Identification of Late Embryogenesis Abundant Proteins
VL  - 43
IS  - 1 (spec. ed.)
SP  - 65
EP  - 65
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4503
ER  - 

@conference{
author = "Pantelić, Ana and Stevanović, Strahinja and Kilibarda, Nataša and Vidović, Marija",
year = "2021",
abstract = "An extreme loss of cellular water or desiccation (5-10% of relative water content) leads to protein denaturation, aggregation and degradation, and affects the fluidity of membrane lipids resulting in loss of membrane integrity [1]. The essential constituents of vegetative desiccation tolerance in so-called resurrection plants are late embryogenesis abundant proteins (LEAPs). This heterogeneous group of anhydrobiosis-related intrinsically disordered proteins forms mostly random conformation when fully hydrated, turning into compact α-helices during desiccation [2]. Based on in vitro studies, LEAPs can be involved in water binding, ion sequestration, stabilization of both membrane and enzymes during freezing or drying, while by forming intracellular proteinaceous condensates they increase structural integrity and intracellular viscosity of cells during desiccation.
Here, we identify 164 members of LEA gene family in endemic and relict resurrection species Ramonda serbica by integrating previously done de novo transcriptome and homologues protein motifs. Identified LEAPs were classification into six groups according to Protein family (PFAM) database and the most populated group was LEA4 containing 47% of total identified LEAPs. By using four secondary structure predictors, we showed that this group exhibited a high propensity to form amphipathic α-helices (81% of total sequence length is predicted to form α-helical structure). This implies that charged residues might be exposed to the solvent, while hydrophobic amino acids might interact with lipid bilayers or with other target proteins in the cell. In addition, as predicted by several bioinformatic tools, more than 70% of identified LEAPs were found to be highly disordered (~64%). Structural characterization of LEAPs is a key to understand their function and regulation of their intrinsic structural disorder-to-order transition during desiccation. These findings will promote transformative advancements in various fields, such as the development of new strategies in neurodegenerative disorders, cell preservation technology and the improvement of crop drought tolerance.",
publisher = "Novi Sad : Faculty of Sciences, Department of Biology and Ecology",
journal = "Biologia Serbica",
title = "De Novo Transcriptome Sequencing of Ramonda serbica: Identification of Late Embryogenesis Abundant Proteins",
volume = "43",
number = "1 (spec. ed.)",
pages = "65-65",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4503"
}

Pantelić, A., Stevanović, S., Kilibarda, N.,& Vidović, M.. (2021). De Novo Transcriptome Sequencing of Ramonda serbica: Identification of Late Embryogenesis Abundant Proteins. in Biologia Serbica
Novi Sad : Faculty of Sciences, Department of Biology and Ecology., 43(1 (spec. ed.)), 65-65.
https://hdl.handle.net/21.15107/rcub_cherry_4503

Pantelić A, Stevanović S, Kilibarda N, Vidović M. De Novo Transcriptome Sequencing of Ramonda serbica: Identification of Late Embryogenesis Abundant Proteins. in Biologia Serbica. 2021;43(1 (spec. ed.)):65-65.
https://hdl.handle.net/21.15107/rcub_cherry_4503 .

Pantelić, Ana, Stevanović, Strahinja, Kilibarda, Nataša, Vidović, Marija, "De Novo Transcriptome Sequencing of Ramonda serbica: Identification of Late Embryogenesis Abundant Proteins" in Biologia Serbica, 43, no. 1 (spec. ed.) (2021):65-65,
https://hdl.handle.net/21.15107/rcub_cherry_4503 .

TY  - CONF
AU  - Vidović, Marija
AU  - Stevanović, Strahinja
AU  - Franchin, Cinzia
AU  - Battisti, Ilaria
AU  - Arrigoni, Giorgio
AU  - Masi, Antonio
AU  - Veljović Jovanović, Sonja
PY  - 2021
UR  - https://inppo.org/inppo2020/
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4424
AB  - Resurrection plant Ramonda serbica Panc. survives desiccation for a long period and fully recovers metabolic functions already within one day upon watering [1]. Besides osmotic stress, desiccation provokes the accelerated generation of reactive oxygen species. The aim of our study was obtaining more insight into the mechanisms of desiccation tolerance in R. serbica by TMT labelled comparative quantitative proteomics of hydrated (HL) and desiccated leaves (DL). After de novo transcriptome analysis, 189456 transcripts with 189003 unigenes were annotated with seven common databases. Proteomic analysis allowed for the relative quantification of 895 different protein groups, 321 with a statistically significant difference in abundance between FL and DL. Among them, 25% referred to chloroplast and almost the same percentage were associated with desiccation and oxidative stress. Almost all differentially abundant proteins related to photosynthetic processes were down-regulated in DL, while those required for protein translation were more abundant in HL. Within differentially abundant proteins involved in antioxidative defence, the levels of enzymes involved in ascorbate-glutathione cycle, peroxiredoxins, Fe and Mn superoxide dismutase (SOD) were all reduced in DL, while germin-like proteins, three Cu/Zn SOD isoforms and polyphenol oxidases were more abundant in DL compared with HL. The protein family with the highest number of members showing the greatest accumulation upon desiccation comprised twenty different late embryogenesis abundant proteins (LEAPs), similarly as found by differential transcriptomic analysis. Taken together, our results imply a key role of LEAPs and Cu/Zn SOD in protective mechanism against desiccation in R. serbica, that may have significant implications on drought-related studies of crops grown in arid areas. This work was supported by the Science Fund of the Republic of Serbia (PROMIS project LEAPSyn-SCI, grant number 6039663). M.V. wishes to acknowledge the support of COST Action BM1405 for approving STSM in Padua during 2017 and 2018.
PB  - International Plant Proteomics Organization
C3  - The Fourth Conference of the International Plant Proteomics Organization
T1  - Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4424
ER  - 

@conference{
author = "Vidović, Marija and Stevanović, Strahinja and Franchin, Cinzia and Battisti, Ilaria and Arrigoni, Giorgio and Masi, Antonio and Veljović Jovanović, Sonja",
year = "2021",
abstract = "Resurrection plant Ramonda serbica Panc. survives desiccation for a long period and fully recovers metabolic functions already within one day upon watering [1]. Besides osmotic stress, desiccation provokes the accelerated generation of reactive oxygen species. The aim of our study was obtaining more insight into the mechanisms of desiccation tolerance in R. serbica by TMT labelled comparative quantitative proteomics of hydrated (HL) and desiccated leaves (DL). After de novo transcriptome analysis, 189456 transcripts with 189003 unigenes were annotated with seven common databases. Proteomic analysis allowed for the relative quantification of 895 different protein groups, 321 with a statistically significant difference in abundance between FL and DL. Among them, 25% referred to chloroplast and almost the same percentage were associated with desiccation and oxidative stress. Almost all differentially abundant proteins related to photosynthetic processes were down-regulated in DL, while those required for protein translation were more abundant in HL. Within differentially abundant proteins involved in antioxidative defence, the levels of enzymes involved in ascorbate-glutathione cycle, peroxiredoxins, Fe and Mn superoxide dismutase (SOD) were all reduced in DL, while germin-like proteins, three Cu/Zn SOD isoforms and polyphenol oxidases were more abundant in DL compared with HL. The protein family with the highest number of members showing the greatest accumulation upon desiccation comprised twenty different late embryogenesis abundant proteins (LEAPs), similarly as found by differential transcriptomic analysis. Taken together, our results imply a key role of LEAPs and Cu/Zn SOD in protective mechanism against desiccation in R. serbica, that may have significant implications on drought-related studies of crops grown in arid areas. This work was supported by the Science Fund of the Republic of Serbia (PROMIS project LEAPSyn-SCI, grant number 6039663). M.V. wishes to acknowledge the support of COST Action BM1405 for approving STSM in Padua during 2017 and 2018.",
publisher = "International Plant Proteomics Organization",
journal = "The Fourth Conference of the International Plant Proteomics Organization",
title = "Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4424"
}

Vidović, M., Stevanović, S., Franchin, C., Battisti, I., Arrigoni, G., Masi, A.,& Veljović Jovanović, S.. (2021). Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves. in The Fourth Conference of the International Plant Proteomics Organization
International Plant Proteomics Organization..
https://hdl.handle.net/21.15107/rcub_cherry_4424

Vidović M, Stevanović S, Franchin C, Battisti I, Arrigoni G, Masi A, Veljović Jovanović S. Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves. in The Fourth Conference of the International Plant Proteomics Organization. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4424 .

Vidović, Marija, Stevanović, Strahinja, Franchin, Cinzia, Battisti, Ilaria, Arrigoni, Giorgio, Masi, Antonio, Veljović Jovanović, Sonja, "Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves" in The Fourth Conference of the International Plant Proteomics Organization (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4424 .

TY  - GEN
AU  - Pantelić, Ana
AU  - Stevanović, Strahinja
AU  - Kilibarda, Nataša
AU  - Vidović, Marija
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4506
PB  - Belgrade BioInformatics
T2  - Belgrade BioInformatics Conference 2021
T1  - De Novo Transcriptome Sequencing of Ramonda serbica : Identification of Late Embryogenesis Abundant Proteins
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4506
ER  - 

@misc{
author = "Pantelić, Ana and Stevanović, Strahinja and Kilibarda, Nataša and Vidović, Marija",
year = "2021",
publisher = "Belgrade BioInformatics",
journal = "Belgrade BioInformatics Conference 2021",
title = "De Novo Transcriptome Sequencing of Ramonda serbica : Identification of Late Embryogenesis Abundant Proteins",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4506"
}

Pantelić, A., Stevanović, S., Kilibarda, N.,& Vidović, M.. (2021). De Novo Transcriptome Sequencing of Ramonda serbica : Identification of Late Embryogenesis Abundant Proteins. in Belgrade BioInformatics Conference 2021
Belgrade BioInformatics..
https://hdl.handle.net/21.15107/rcub_cherry_4506

Pantelić A, Stevanović S, Kilibarda N, Vidović M. De Novo Transcriptome Sequencing of Ramonda serbica : Identification of Late Embryogenesis Abundant Proteins. in Belgrade BioInformatics Conference 2021. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4506 .

Pantelić, Ana, Stevanović, Strahinja, Kilibarda, Nataša, Vidović, Marija, "De Novo Transcriptome Sequencing of Ramonda serbica : Identification of Late Embryogenesis Abundant Proteins" in Belgrade BioInformatics Conference 2021 (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4506 .

TY  - CONF
AU  - Stevanović, Strahinja
AU  - Vidović, Marija
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4508
AB  - Desiccation or extreme water loss leads to protein denaturation, aggregation, and degradation and impairs membrane lipid fluidity, resulting in loss of membrane integrity at the cellular level. The induction of late embryogenesis abundant proteins (LEAPs) is considered an essential component of desiccation tolerance strategy in so-called resurrection plants. This heterogeneous group of hydrophilic, non-globular proteins is characterised by a high structural plasticity that allows them to adopt a random conformation in aqueous solutions that transforms into α-helices during dehydration [1]. Therefore, LEAPs can interact with various ligands and partners, including ion sequestration and stabilisation of membranes and enzymes during freezing or drying [2].
Our new transcriptome database of an endemic resurrection species Ramonda serbica allowed us to identify 164 members of the LEA gene family. LEAPs of this sample data have an average primary sequence similarity and identity of 10% and 6%, respectively, but with a high variance (141 and 108), which means that the sample proteins can be classified based on domain homology. The averaging is based on multiple sequence alignment and the variance is estimated using pairwise sequence alignment scores. Accordingly, all identified LEAPs were clustered into six groups based on protein families (PFAM). Among these groups, LEAPs differ significantly in their secondary structure, disorder propensity and aggregation potential. Furthermore, we built homology models using PDB structures as templates. For each group, an ensemble of superimposed 3D homology models was analyzed. 
The information obtained from the representative structural models is key to understanding the function of LEAPs and the regulation of their intrinsic structural disorder-to-order transition during desiccation. This will pave the way for the identification of LEAPs endogenous partners and their targets in the cell and provide further insights into the protective mechanisms of desiccation tolerance.
C3  - Virtual symposium celebrating the 50th anniversary of the Protein Data Bank, May 4–5
T1  - In silico structural survey of newly identified late embryogenesis abundant proteins (LEAPs) from Ramonda serbica and their structure - function relationship
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4508
ER  - 

@conference{
author = "Stevanović, Strahinja and Vidović, Marija",
year = "2021",
abstract = "Desiccation or extreme water loss leads to protein denaturation, aggregation, and degradation and impairs membrane lipid fluidity, resulting in loss of membrane integrity at the cellular level. The induction of late embryogenesis abundant proteins (LEAPs) is considered an essential component of desiccation tolerance strategy in so-called resurrection plants. This heterogeneous group of hydrophilic, non-globular proteins is characterised by a high structural plasticity that allows them to adopt a random conformation in aqueous solutions that transforms into α-helices during dehydration [1]. Therefore, LEAPs can interact with various ligands and partners, including ion sequestration and stabilisation of membranes and enzymes during freezing or drying [2].
Our new transcriptome database of an endemic resurrection species Ramonda serbica allowed us to identify 164 members of the LEA gene family. LEAPs of this sample data have an average primary sequence similarity and identity of 10% and 6%, respectively, but with a high variance (141 and 108), which means that the sample proteins can be classified based on domain homology. The averaging is based on multiple sequence alignment and the variance is estimated using pairwise sequence alignment scores. Accordingly, all identified LEAPs were clustered into six groups based on protein families (PFAM). Among these groups, LEAPs differ significantly in their secondary structure, disorder propensity and aggregation potential. Furthermore, we built homology models using PDB structures as templates. For each group, an ensemble of superimposed 3D homology models was analyzed. 
The information obtained from the representative structural models is key to understanding the function of LEAPs and the regulation of their intrinsic structural disorder-to-order transition during desiccation. This will pave the way for the identification of LEAPs endogenous partners and their targets in the cell and provide further insights into the protective mechanisms of desiccation tolerance.",
journal = "Virtual symposium celebrating the 50th anniversary of the Protein Data Bank, May 4–5",
title = "In silico structural survey of newly identified late embryogenesis abundant proteins (LEAPs) from Ramonda serbica and their structure - function relationship",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4508"
}

Stevanović, S.,& Vidović, M.. (2021). In silico structural survey of newly identified late embryogenesis abundant proteins (LEAPs) from Ramonda serbica and their structure - function relationship. in Virtual symposium celebrating the 50th anniversary of the Protein Data Bank, May 4–5.
https://hdl.handle.net/21.15107/rcub_cherry_4508

Stevanović S, Vidović M. In silico structural survey of newly identified late embryogenesis abundant proteins (LEAPs) from Ramonda serbica and their structure - function relationship. in Virtual symposium celebrating the 50th anniversary of the Protein Data Bank, May 4–5. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4508 .

Stevanović, Strahinja, Vidović, Marija, "In silico structural survey of newly identified late embryogenesis abundant proteins (LEAPs) from Ramonda serbica and their structure - function relationship" in Virtual symposium celebrating the 50th anniversary of the Protein Data Bank, May 4–5 (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4508 .

TY  - CONF
AU  - Stevanović, Strahinja
AU  - Vidović, Marija
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4649
AB  - Desiccation or extreme water loss leads to protein denaturation, aggregation, and degradation and impairs membrane lipid fluidity, resulting in loss of membrane integrity at the cellular level. The induction of late embryogenesis abundant proteins (LEAPs) is considered an essential component of desiccation tolerance strategy in so-called resurrection plants. This heterogeneous group of hydrophilic, non-globular proteins is characterized by a high structural plasticity that allows them to adopt a random conformation in aqueous solutions that transforms into α-helices during dehydration [1]. Therefore, LEAPs can interact with various ligands and partners, including ion sequestration and stabilization of membranes and enzymes during freezing or drying [2]. Our new transcriptome database of an endemic resurrection species Ramonda serbica allowed us to identify 153 members of the LEA gene family. LEAPs of this sample data have an average primary sequence similarity and identity of 10% and 6%, respectively, but with a high variance (141 and 108), which means that the sample proteins can be classified based on domain homology. The averaging is based on multiple sequence alignment and the variance is estimated using pairwise sequence alignment scores. Accordingly, all identified LEAPs were clustered into six groups based on protein families (PFAM). Among these groups, LEAPs differ significantly in their secondary structure, disorder propensity and aggregation potential. Furthermore, we built homology models using Protein Data Bank structure information as templates. For each group, an ensemble of superimposed 3D homology models was analyzed. The information obtained from the representative structural models is key to understanding the function of LEAPs and the regulation of their intrinsic structural disorder-to-order transition during desiccation. This will pave the way for the identification of LEAPs endogenous partners and their targets in the cell and provide further insights into the protective mechanisms of desiccation tolerance.
C3  - Virtual symposium celebrating the 50th anniversary of the Protein Data Bank, May 4–5
T1  - In silico structural survey of newly identified late embryogenesis abundant proteins (LEAPs) from Ramonda serbica and their structure - function relationship
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4649
ER  - 

@conference{
author = "Stevanović, Strahinja and Vidović, Marija",
year = "2021",
abstract = "Desiccation or extreme water loss leads to protein denaturation, aggregation, and degradation and impairs membrane lipid fluidity, resulting in loss of membrane integrity at the cellular level. The induction of late embryogenesis abundant proteins (LEAPs) is considered an essential component of desiccation tolerance strategy in so-called resurrection plants. This heterogeneous group of hydrophilic, non-globular proteins is characterized by a high structural plasticity that allows them to adopt a random conformation in aqueous solutions that transforms into α-helices during dehydration [1]. Therefore, LEAPs can interact with various ligands and partners, including ion sequestration and stabilization of membranes and enzymes during freezing or drying [2]. Our new transcriptome database of an endemic resurrection species Ramonda serbica allowed us to identify 153 members of the LEA gene family. LEAPs of this sample data have an average primary sequence similarity and identity of 10% and 6%, respectively, but with a high variance (141 and 108), which means that the sample proteins can be classified based on domain homology. The averaging is based on multiple sequence alignment and the variance is estimated using pairwise sequence alignment scores. Accordingly, all identified LEAPs were clustered into six groups based on protein families (PFAM). Among these groups, LEAPs differ significantly in their secondary structure, disorder propensity and aggregation potential. Furthermore, we built homology models using Protein Data Bank structure information as templates. For each group, an ensemble of superimposed 3D homology models was analyzed. The information obtained from the representative structural models is key to understanding the function of LEAPs and the regulation of their intrinsic structural disorder-to-order transition during desiccation. This will pave the way for the identification of LEAPs endogenous partners and their targets in the cell and provide further insights into the protective mechanisms of desiccation tolerance.",
journal = "Virtual symposium celebrating the 50th anniversary of the Protein Data Bank, May 4–5",
title = "In silico structural survey of newly identified late embryogenesis abundant proteins (LEAPs) from Ramonda serbica and their structure - function relationship",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4649"
}

Stevanović, S.,& Vidović, M.. (2021). In silico structural survey of newly identified late embryogenesis abundant proteins (LEAPs) from Ramonda serbica and their structure - function relationship. in Virtual symposium celebrating the 50th anniversary of the Protein Data Bank, May 4–5.
https://hdl.handle.net/21.15107/rcub_cherry_4649

Stevanović S, Vidović M. In silico structural survey of newly identified late embryogenesis abundant proteins (LEAPs) from Ramonda serbica and their structure - function relationship. in Virtual symposium celebrating the 50th anniversary of the Protein Data Bank, May 4–5. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4649 .

Stevanović, Strahinja, Vidović, Marija, "In silico structural survey of newly identified late embryogenesis abundant proteins (LEAPs) from Ramonda serbica and their structure - function relationship" in Virtual symposium celebrating the 50th anniversary of the Protein Data Bank, May 4–5 (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4649 .