TY  - JOUR
AU  - Dimitrijevic, R.
AU  - Cvetković, Olga
AU  - Miodragović, Zoran
AU  - Simić, Miloš

AU  - Manojlović, Dragan D.
AU  - Jovic, V.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1460
AB  - The Ag nano-structured thin films prepared on flat glass substrates have been studied. The ball-like silver nanoparticles have been synthesized in large quantity by using a modified method of hydrolytic decomposition of silver complexes with amino types ligands formed in ethanol aqueous solution. SEM analysis revealed that Ag nanoparticles are all sphere shaped with bimodal size (40 and 70 nm) distribution. The results of XRD powder pattern examination show that Ag nanoparticles are pure phase, well crystallized. The unit cell dimensions measured on synthesized Ag nano films show small but frequent contraction in comparison to Ag metal standard.
PB  - Technical Faculty, Bor-Serbia, Bor
T2  - Journal of mining and metallurgy, Section B: Metallurgy
T1  - Sem/Edx and Xrd Characterization of Silver Nanocrystalline Thin Film Prepared from  Organometallic Solution Precursor
VL  - 49
IS  - 1
SP  - 91
EP  - 95
DO  - 10.2298/JMMB120111041D
ER  - 

@article{
author = "Dimitrijevic, R. and Cvetković, Olga and Miodragović, Zoran and Simić, Miloš
 and Manojlović, Dragan D. and Jovic, V.",
year = "2013",
abstract = "The Ag nano-structured thin films prepared on flat glass substrates have been studied. The ball-like silver nanoparticles have been synthesized in large quantity by using a modified method of hydrolytic decomposition of silver complexes with amino types ligands formed in ethanol aqueous solution. SEM analysis revealed that Ag nanoparticles are all sphere shaped with bimodal size (40 and 70 nm) distribution. The results of XRD powder pattern examination show that Ag nanoparticles are pure phase, well crystallized. The unit cell dimensions measured on synthesized Ag nano films show small but frequent contraction in comparison to Ag metal standard.",
publisher = "Technical Faculty, Bor-Serbia, Bor",
journal = "Journal of mining and metallurgy, Section B: Metallurgy",
title = "Sem/Edx and Xrd Characterization of Silver Nanocrystalline Thin Film Prepared from  Organometallic Solution Precursor",
volume = "49",
number = "1",
pages = "91-95",
doi = "10.2298/JMMB120111041D"
}

Dimitrijevic, R., Cvetković, O., Miodragović, Z., Simić, M., Manojlović, D. D.,& Jovic, V.. (2013). Sem/Edx and Xrd Characterization of Silver Nanocrystalline Thin Film Prepared from  Organometallic Solution Precursor. in Journal of mining and metallurgy, Section B: Metallurgy
Technical Faculty, Bor-Serbia, Bor., 49(1), 91-95.
https://doi.org/10.2298/JMMB120111041D

Dimitrijevic R, Cvetković O, Miodragović Z, Simić M, Manojlović DD, Jovic V. Sem/Edx and Xrd Characterization of Silver Nanocrystalline Thin Film Prepared from  Organometallic Solution Precursor. in Journal of mining and metallurgy, Section B: Metallurgy. 2013;49(1):91-95.
doi:10.2298/JMMB120111041D .

Dimitrijevic, R., Cvetković, Olga, Miodragović, Zoran, Simić, Miloš
, Manojlović, Dragan D., Jovic, V., "Sem/Edx and Xrd Characterization of Silver Nanocrystalline Thin Film Prepared from  Organometallic Solution Precursor" in Journal of mining and metallurgy, Section B: Metallurgy, 49, no. 1 (2013):91-95,
https://doi.org/10.2298/JMMB120111041D . .

TY  - JOUR
AU  - Dimitrijevic, R.
AU  - Stojanovic, M.
AU  - Micic, M.
AU  - Dimitrijevic, Lj
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1310
AB  - To explore the potential usage of recombinant banana lectin as an immunostimulator it was of interest to analyze the effect it exerted in vivo in mice, upon two different routes of exposure. By Western blotting analysis of the gastric and intestinal luminal content it was found that recombinant banana lectin is stable in vivo in the mouse digestive tract, where it specifically interacts with the mucosal surfaces which can be inhibited by the addition of glucose. Its attachment to mice jejunum has been confirmed by immunofluorescence. In addition, it was able to induce systemic immunity, evidenced by specific antibody production, by oral application, a property that might be exploited for the induction of systemic immune responses. (c) 2012 Elsevier Ltd. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Functional Foods
T1  - Recombinant banana lectin as mucosal immunostimulator
VL  - 4
IS  - 3
SP  - 636
EP  - 641
DO  - 10.1016/j.jff.2012.04.003
ER  - 

@article{
author = "Dimitrijevic, R. and Stojanovic, M. and Micic, M. and Dimitrijevic, Lj and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "To explore the potential usage of recombinant banana lectin as an immunostimulator it was of interest to analyze the effect it exerted in vivo in mice, upon two different routes of exposure. By Western blotting analysis of the gastric and intestinal luminal content it was found that recombinant banana lectin is stable in vivo in the mouse digestive tract, where it specifically interacts with the mucosal surfaces which can be inhibited by the addition of glucose. Its attachment to mice jejunum has been confirmed by immunofluorescence. In addition, it was able to induce systemic immunity, evidenced by specific antibody production, by oral application, a property that might be exploited for the induction of systemic immune responses. (c) 2012 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Functional Foods",
title = "Recombinant banana lectin as mucosal immunostimulator",
volume = "4",
number = "3",
pages = "636-641",
doi = "10.1016/j.jff.2012.04.003"
}

Dimitrijevic, R., Stojanovic, M., Micic, M., Dimitrijevic, L.,& Gavrović-Jankulović, M.. (2012). Recombinant banana lectin as mucosal immunostimulator. in Journal of Functional Foods
Elsevier Science Bv, Amsterdam., 4(3), 636-641.
https://doi.org/10.1016/j.jff.2012.04.003

Dimitrijevic R, Stojanovic M, Micic M, Dimitrijevic L, Gavrović-Jankulović M. Recombinant banana lectin as mucosal immunostimulator. in Journal of Functional Foods. 2012;4(3):636-641.
doi:10.1016/j.jff.2012.04.003 .

Dimitrijevic, R., Stojanovic, M., Micic, M., Dimitrijevic, Lj, Gavrović-Jankulović, Marija, "Recombinant banana lectin as mucosal immunostimulator" in Journal of Functional Foods, 4, no. 3 (2012):636-641,
https://doi.org/10.1016/j.jff.2012.04.003 . .

TY  - CONF
AU  - Abughren, Salem Alzwam M.
AU  - Dimitrijevic, R.
AU  - Popović, Milica M.
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1471
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Production and characterisation of recombinant banana glucanase
VL  - 66
SP  - 391
EP  - 391
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1471
ER  - 

@conference{
author = "Abughren, Salem Alzwam M. and Dimitrijevic, R. and Popović, Milica M. and Atanasković-Marković, Marina and Gavrović-Jankulović, Marija",
year = "2011",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Production and characterisation of recombinant banana glucanase",
volume = "66",
pages = "391-391",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1471"
}

Abughren, S. A. M., Dimitrijevic, R., Popović, M. M., Atanasković-Marković, M.,& Gavrović-Jankulović, M.. (2011). Production and characterisation of recombinant banana glucanase. in Allergy
Wiley-Blackwell, Hoboken., 66, 391-391.
https://hdl.handle.net/21.15107/rcub_cherry_1471

Abughren SAM, Dimitrijevic R, Popović MM, Atanasković-Marković M, Gavrović-Jankulović M. Production and characterisation of recombinant banana glucanase. in Allergy. 2011;66:391-391.
https://hdl.handle.net/21.15107/rcub_cherry_1471 .

Abughren, Salem Alzwam M., Dimitrijevic, R., Popović, Milica M., Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, "Production and characterisation of recombinant banana glucanase" in Allergy, 66 (2011):391-391,
https://hdl.handle.net/21.15107/rcub_cherry_1471 .

TY  - CHAP
AU  - Gavrović-Jankulović, Marija
AU  - Dimitrijevic, R.
AU  - Stojanovic, M.
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/123
AB  - Lectins are a highly diverse group of proteins whose biological functions have been associated with the carbohydrate binding activities. Banana lectin is a member of the jacalin-related family of lectins, and belongs to the glucose/mannose specific subgroup. However, it shows a unique specificity for internal α1,3 linkages as well as β1,3 linkages at the reducing termini in branched mannose oligosaccharides, which are components of the-core region of N-linked glycoproteins. As some other plant lectins, banana lectin is stable to the harsh conditions of the human gastrointestinal tract. As a small protein it seems to be able to pass the mucosal barrier and to reach the immune system inducing specific IgG4 antibodies. Banana lectin also displays T cell proliferation in CD3+, CD4+ and CD8+ populations of human PBMCs. It has been recently shown that in vitro stimulation of Balb/c and C57 BL/6 splenocytes by the recombinantly produced banana lectin resulted in the proliferation of T cells and an increased secretion of interferon-gamma. Due to its notable immunomodulatory potential, it has been proposed for the treatment of some Th2-related disorders. This work will discuss banana lectin interactions with the immune system and consider implications for future therapeutic applications.
T2  - Bananas: Nutrition, Diseases and Trade Issues
T1  - Banana lectin interactions with the immune system: Implications for future therapeutic applications
SP  - 307
EP  - 318
UR  - https://hdl.handle.net/21.15107/rcub_cherry_123
ER  - 

@inbook{
author = "Gavrović-Jankulović, Marija and Dimitrijevic, R. and Stojanovic, M.",
year = "2011",
abstract = "Lectins are a highly diverse group of proteins whose biological functions have been associated with the carbohydrate binding activities. Banana lectin is a member of the jacalin-related family of lectins, and belongs to the glucose/mannose specific subgroup. However, it shows a unique specificity for internal α1,3 linkages as well as β1,3 linkages at the reducing termini in branched mannose oligosaccharides, which are components of the-core region of N-linked glycoproteins. As some other plant lectins, banana lectin is stable to the harsh conditions of the human gastrointestinal tract. As a small protein it seems to be able to pass the mucosal barrier and to reach the immune system inducing specific IgG4 antibodies. Banana lectin also displays T cell proliferation in CD3+, CD4+ and CD8+ populations of human PBMCs. It has been recently shown that in vitro stimulation of Balb/c and C57 BL/6 splenocytes by the recombinantly produced banana lectin resulted in the proliferation of T cells and an increased secretion of interferon-gamma. Due to its notable immunomodulatory potential, it has been proposed for the treatment of some Th2-related disorders. This work will discuss banana lectin interactions with the immune system and consider implications for future therapeutic applications.",
journal = "Bananas: Nutrition, Diseases and Trade Issues",
booktitle = "Banana lectin interactions with the immune system: Implications for future therapeutic applications",
pages = "307-318",
url = "https://hdl.handle.net/21.15107/rcub_cherry_123"
}

Gavrović-Jankulović, M., Dimitrijevic, R.,& Stojanovic, M.. (2011). Banana lectin interactions with the immune system: Implications for future therapeutic applications. in Bananas: Nutrition, Diseases and Trade Issues, 307-318.
https://hdl.handle.net/21.15107/rcub_cherry_123

Gavrović-Jankulović M, Dimitrijevic R, Stojanovic M. Banana lectin interactions with the immune system: Implications for future therapeutic applications. in Bananas: Nutrition, Diseases and Trade Issues. 2011;:307-318.
https://hdl.handle.net/21.15107/rcub_cherry_123 .

Gavrović-Jankulović, Marija, Dimitrijevic, R., Stojanovic, M., "Banana lectin interactions with the immune system: Implications for future therapeutic applications" in Bananas: Nutrition, Diseases and Trade Issues (2011):307-318,
https://hdl.handle.net/21.15107/rcub_cherry_123 .

TY  - JOUR
AU  - Dimitrijevic, R.
AU  - Stojanovic, M.
AU  - Živković, Irena
AU  - Petersen, A.
AU  - Jankov, Ratko M.
AU  - Dimitrijevic, L.
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1028
AB  - Aims: This study focuses on the isolation and characterization of a peptide with bacteriocin-like properties isolated from Lactobacillus rhamnosus strain 68, previously identified by 16S rRNA gene sequencing and originating from human gastrointestinal flora. Methods and Results: The peptide was isolated from a supernatant of bacteria maintained under restrictive conditions by a combination of ethanol precipitation and reversed-phase chromatography. The molecular mass of the peptide as assessed by mass spectrometry was 6433 center dot 8 Da. An isoelectric point of 9 center dot 8 was determined by 2D-PAGE. The peptide designated rhamnosin A inhibited Micrococcus lysodeikticus ATCC 4698 but did not inhibit Lactobacillus plantarum 8014 or Lact. plantarum 39268. Inhibitory activity against M. lysodeikticus at concentrations used in this study was shown to be bacteriostatic rather than bacteriolytic or bactericidal. Rhamnosin A retained biological activity after heat treatment (95 degrees C, 30 min) but was sensitive to proteolytic activity of pepsin and trypsin. Conclusions: The N-terminal sequence of rhamnosin A, as determined by Edman degradation and in more detail by blast analysis, did not show identity with any currently available Lact. rhamnosus HN001-translated protein sequences, nor any significant similarity with other sequences in the nonredundant protein sequence database. Being a small, heat-stable, nonlanthionine-containing peptide, rhamnosin A should be categorized as a class II bacteriocin. Significance and Impact of the Study: This study describes a partial bacteriocin sequence isolated from Lact. rhamnosus 68 and broadens our understanding of bacteriocins.
PB  - Wiley-Blackwell, Hoboken
T2  - Journal of Applied Microbiology
T1  - The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68
VL  - 107
IS  - 6
SP  - 2108
EP  - 2115
DO  - 10.1111/j.1365-2672.2009.04539.x
ER  - 

@article{
author = "Dimitrijevic, R. and Stojanovic, M. and Živković, Irena and Petersen, A. and Jankov, Ratko M. and Dimitrijevic, L. and Gavrović-Jankulović, Marija",
year = "2009",
abstract = "Aims: This study focuses on the isolation and characterization of a peptide with bacteriocin-like properties isolated from Lactobacillus rhamnosus strain 68, previously identified by 16S rRNA gene sequencing and originating from human gastrointestinal flora. Methods and Results: The peptide was isolated from a supernatant of bacteria maintained under restrictive conditions by a combination of ethanol precipitation and reversed-phase chromatography. The molecular mass of the peptide as assessed by mass spectrometry was 6433 center dot 8 Da. An isoelectric point of 9 center dot 8 was determined by 2D-PAGE. The peptide designated rhamnosin A inhibited Micrococcus lysodeikticus ATCC 4698 but did not inhibit Lactobacillus plantarum 8014 or Lact. plantarum 39268. Inhibitory activity against M. lysodeikticus at concentrations used in this study was shown to be bacteriostatic rather than bacteriolytic or bactericidal. Rhamnosin A retained biological activity after heat treatment (95 degrees C, 30 min) but was sensitive to proteolytic activity of pepsin and trypsin. Conclusions: The N-terminal sequence of rhamnosin A, as determined by Edman degradation and in more detail by blast analysis, did not show identity with any currently available Lact. rhamnosus HN001-translated protein sequences, nor any significant similarity with other sequences in the nonredundant protein sequence database. Being a small, heat-stable, nonlanthionine-containing peptide, rhamnosin A should be categorized as a class II bacteriocin. Significance and Impact of the Study: This study describes a partial bacteriocin sequence isolated from Lact. rhamnosus 68 and broadens our understanding of bacteriocins.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Journal of Applied Microbiology",
title = "The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68",
volume = "107",
number = "6",
pages = "2108-2115",
doi = "10.1111/j.1365-2672.2009.04539.x"
}

Dimitrijevic, R., Stojanovic, M., Živković, I., Petersen, A., Jankov, R. M., Dimitrijevic, L.,& Gavrović-Jankulović, M.. (2009). The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68. in Journal of Applied Microbiology
Wiley-Blackwell, Hoboken., 107(6), 2108-2115.
https://doi.org/10.1111/j.1365-2672.2009.04539.x

Dimitrijevic R, Stojanovic M, Živković I, Petersen A, Jankov RM, Dimitrijevic L, Gavrović-Jankulović M. The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68. in Journal of Applied Microbiology. 2009;107(6):2108-2115.
doi:10.1111/j.1365-2672.2009.04539.x .

Dimitrijevic, R., Stojanovic, M., Živković, Irena, Petersen, A., Jankov, Ratko M., Dimitrijevic, L., Gavrović-Jankulović, Marija, "The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68" in Journal of Applied Microbiology, 107, no. 6 (2009):2108-2115,
https://doi.org/10.1111/j.1365-2672.2009.04539.x . .

TY  - JOUR
AU  - Minić, Dragica M.
AU  - Susic, M
AU  - Tešić, Živoslav Lj.
AU  - Dimitrijevic, R
PY  - 1997
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/365
AB  - It was shown by differential scanning calorimetry and X-ray diffraction that chemically prepared Ag-Pd intermetallic compounds of different composition in powder form are active hydrogen absorbers in the temperature range 20-300 degrees C. During thermal treatment in vacuum transition into crystalline state takes place. The process of hydrogen absorption was analysed and thermodynamic and kinetic parameters of this process determined.
PB  - Elsevier Science Publ B V, Amsterdam
T2  - Studies in Surface Science and Catalysis
T1  - Investigation of the thermal behaviour of Ag-Pd intermetallic compounds in hydrogen atmosphere
VL  - 112
SP  - 447
EP  - 456
DO  - 10.1016/S0167-2991(97)80868-3
ER  - 

@article{
author = "Minić, Dragica M. and Susic, M and Tešić, Živoslav Lj. and Dimitrijevic, R",
year = "1997",
abstract = "It was shown by differential scanning calorimetry and X-ray diffraction that chemically prepared Ag-Pd intermetallic compounds of different composition in powder form are active hydrogen absorbers in the temperature range 20-300 degrees C. During thermal treatment in vacuum transition into crystalline state takes place. The process of hydrogen absorption was analysed and thermodynamic and kinetic parameters of this process determined.",
publisher = "Elsevier Science Publ B V, Amsterdam",
journal = "Studies in Surface Science and Catalysis",
title = "Investigation of the thermal behaviour of Ag-Pd intermetallic compounds in hydrogen atmosphere",
volume = "112",
pages = "447-456",
doi = "10.1016/S0167-2991(97)80868-3"
}

Minić, D. M., Susic, M., Tešić, Ž. Lj.,& Dimitrijevic, R.. (1997). Investigation of the thermal behaviour of Ag-Pd intermetallic compounds in hydrogen atmosphere. in Studies in Surface Science and Catalysis
Elsevier Science Publ B V, Amsterdam., 112, 447-456.
https://doi.org/10.1016/S0167-2991(97)80868-3

Minić DM, Susic M, Tešić ŽL, Dimitrijevic R. Investigation of the thermal behaviour of Ag-Pd intermetallic compounds in hydrogen atmosphere. in Studies in Surface Science and Catalysis. 1997;112:447-456.
doi:10.1016/S0167-2991(97)80868-3 .

Minić, Dragica M., Susic, M, Tešić, Živoslav Lj., Dimitrijevic, R, "Investigation of the thermal behaviour of Ag-Pd intermetallic compounds in hydrogen atmosphere" in Studies in Surface Science and Catalysis, 112 (1997):447-456,
https://doi.org/10.1016/S0167-2991(97)80868-3 . .