TY  - JOUR
AU  - Glišić, Sanja
AU  - Arrigo, Patrizio
AU  - Alavantić, Dragan
AU  - Perović, Vladimir R.
AU  - Prljić, Jelena
AU  - Veljković, Nevena V.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3356
AB  - Lipoprotein lipase (LPL) is a key enzyme in lipid metabolism. Decrease of the LPL enzymatic activity leads to elevated triglycerides (TG) and reduced high-density lipoprotein (HDL-C levels), both risk factors for cardiovascular disease (CVD). Therefore, mutations, which decrease the LPL activity, may confer susceptibility to CVD. Here, the informational spectrum method (ISM), a virtual spectroscopy method for structure/function analysis of nucleotide and protein sequences, is applied for identification of evolutionary highly conserved information encoded by the primary structure of LPL. It was demonstrated that mutations, which alter the LPL enzymatic activity also alter this information. On the basis of this finding, an efficient an simple bioinformatics criterion for assessment of the pathogenic effect of LPL nonsynonymous single nucleotide substitution as a risk factor of CVD has been proposed.
T2  - Proteins: Structure Function and Bioinformatics
T1  - Lipoprotein lipase: A bioinformatics criterion for assessment of mutations as a risk factor for cardiovascular disease
VL  - 70
IS  - 3
SP  - 855
EP  - 862
DO  - 10.1002/prot.21581
ER  - 

@article{
author = "Glišić, Sanja and Arrigo, Patrizio and Alavantić, Dragan and Perović, Vladimir R. and Prljić, Jelena and Veljković, Nevena V.",
year = "2008",
abstract = "Lipoprotein lipase (LPL) is a key enzyme in lipid metabolism. Decrease of the LPL enzymatic activity leads to elevated triglycerides (TG) and reduced high-density lipoprotein (HDL-C levels), both risk factors for cardiovascular disease (CVD). Therefore, mutations, which decrease the LPL activity, may confer susceptibility to CVD. Here, the informational spectrum method (ISM), a virtual spectroscopy method for structure/function analysis of nucleotide and protein sequences, is applied for identification of evolutionary highly conserved information encoded by the primary structure of LPL. It was demonstrated that mutations, which alter the LPL enzymatic activity also alter this information. On the basis of this finding, an efficient an simple bioinformatics criterion for assessment of the pathogenic effect of LPL nonsynonymous single nucleotide substitution as a risk factor of CVD has been proposed.",
journal = "Proteins: Structure Function and Bioinformatics",
title = "Lipoprotein lipase: A bioinformatics criterion for assessment of mutations as a risk factor for cardiovascular disease",
volume = "70",
number = "3",
pages = "855-862",
doi = "10.1002/prot.21581"
}

Glišić, S., Arrigo, P., Alavantić, D., Perović, V. R., Prljić, J.,& Veljković, N. V.. (2008). Lipoprotein lipase: A bioinformatics criterion for assessment of mutations as a risk factor for cardiovascular disease. in Proteins: Structure Function and Bioinformatics, 70(3), 855-862.
https://doi.org/10.1002/prot.21581

Glišić S, Arrigo P, Alavantić D, Perović VR, Prljić J, Veljković NV. Lipoprotein lipase: A bioinformatics criterion for assessment of mutations as a risk factor for cardiovascular disease. in Proteins: Structure Function and Bioinformatics. 2008;70(3):855-862.
doi:10.1002/prot.21581 .

Glišić, Sanja, Arrigo, Patrizio, Alavantić, Dragan, Perović, Vladimir R., Prljić, Jelena, Veljković, Nevena V., "Lipoprotein lipase: A bioinformatics criterion for assessment of mutations as a risk factor for cardiovascular disease" in Proteins: Structure Function and Bioinformatics, 70, no. 3 (2008):855-862,
https://doi.org/10.1002/prot.21581 . .

TY  - JOUR
AU  - Veljković, Nevena V.
AU  - Glišić, Sanja
AU  - Prljić, Jelena
AU  - Perović, Vladimir R.
AU  - Botta, Maurizio
AU  - Veljković, Veljko
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3544
AB  - The field of bioinformatics has become a major part of the drug discovery pipeline playing a key role in improvement and acceleration of this time and money consuming process. Here we review the application of the informational spectrum method ( ISM), a virtual spectroscopy method for structure/function analysis of proteins, in identification of functional protein domains representing candidate therapeutic targets for drugs against human immunodeficiency virus (HIV)-1, anthrax, highly pathogenic influenza virus H5N1 and cardiovascular diseases.
T2  - Current Protein and Peptide Science
T1  - Discovery of New Therapeutic Targets by the Informational Spectrum Method
VL  - 9
IS  - 5
SP  - 493
EP  - 506
DO  - 10.2174/138920308785915245
ER  - 

@article{
author = "Veljković, Nevena V. and Glišić, Sanja and Prljić, Jelena and Perović, Vladimir R. and Botta, Maurizio and Veljković, Veljko",
year = "2008",
abstract = "The field of bioinformatics has become a major part of the drug discovery pipeline playing a key role in improvement and acceleration of this time and money consuming process. Here we review the application of the informational spectrum method ( ISM), a virtual spectroscopy method for structure/function analysis of proteins, in identification of functional protein domains representing candidate therapeutic targets for drugs against human immunodeficiency virus (HIV)-1, anthrax, highly pathogenic influenza virus H5N1 and cardiovascular diseases.",
journal = "Current Protein and Peptide Science",
title = "Discovery of New Therapeutic Targets by the Informational Spectrum Method",
volume = "9",
number = "5",
pages = "493-506",
doi = "10.2174/138920308785915245"
}

Veljković, N. V., Glišić, S., Prljić, J., Perović, V. R., Botta, M.,& Veljković, V.. (2008). Discovery of New Therapeutic Targets by the Informational Spectrum Method. in Current Protein and Peptide Science, 9(5), 493-506.
https://doi.org/10.2174/138920308785915245

Veljković NV, Glišić S, Prljić J, Perović VR, Botta M, Veljković V. Discovery of New Therapeutic Targets by the Informational Spectrum Method. in Current Protein and Peptide Science. 2008;9(5):493-506.
doi:10.2174/138920308785915245 .

Veljković, Nevena V., Glišić, Sanja, Prljić, Jelena, Perović, Vladimir R., Botta, Maurizio, Veljković, Veljko, "Discovery of New Therapeutic Targets by the Informational Spectrum Method" in Current Protein and Peptide Science, 9, no. 5 (2008):493-506,
https://doi.org/10.2174/138920308785915245 . .

TY  - JOUR
AU  - Đorđević, Ana
AU  - Veljković, Milena
AU  - Antoni, Sascha
AU  - Sakarellos-Daitsiotis, Maria
AU  - Krikorian, Dimitrios
AU  - Zevgiti, Stella
AU  - Dietrich, Ursula
AU  - Veljković, Nevena V.
AU  - Branch, Donald R.
PY  - 2007
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3295
AB  - The C-terminus of the second conserved region of HIV-1 gp120 represents a functionally important domain, as it encompasses amino acids directly involved in the binding to the CD4 receptor and in post-receptor binding events. Previous studies have suggested that antibodies with specific affinity to a 23 amino acids-long NTM polypeptide, derived from this HIV-1 gp120 domain, may be involved in the control of HIV disease progression. In the current work, we searched for NTM-recognizing antibodies in specific cohorts of HIV-1 infected individuals, including long-term non-progressors (LTNP) and progressors. For this purpose, we employed a previously defined bioinformatics criterion for design of an NTM peptide mimetic to select an octapeptide, NTMs (FTDNAKTI), which is more suitable for use in a solid-state enzyme-linked immunosorbent assay (ELISA). Our results show that NTMs-reactive antibodies are significantly more prevalent (p LT 0.01) in LTNP as compared to progressors and healthy control subjects, indicating their association with non-progressive infection. The presence of antibodies recognizing the second conserved region of the HIV-1 gp120 derived peptide, NTMs, in LTNP sera suggest that these antibodies could be of considerable interest for development of anti-HIV immune-based therapies and vaccines.
T2  - Current HIV Research
T1  - The presence of antibodies recognizing a peptide derived from the second conserved region of HIV-1 gp120 correlates with non-progressive HIV infection
VL  - 5
IS  - 5
SP  - 443
EP  - 448
DO  - 10.2174/157016207781662470
ER  - 

@article{
author = "Đorđević, Ana and Veljković, Milena and Antoni, Sascha and Sakarellos-Daitsiotis, Maria and Krikorian, Dimitrios and Zevgiti, Stella and Dietrich, Ursula and Veljković, Nevena V. and Branch, Donald R.",
year = "2007",
abstract = "The C-terminus of the second conserved region of HIV-1 gp120 represents a functionally important domain, as it encompasses amino acids directly involved in the binding to the CD4 receptor and in post-receptor binding events. Previous studies have suggested that antibodies with specific affinity to a 23 amino acids-long NTM polypeptide, derived from this HIV-1 gp120 domain, may be involved in the control of HIV disease progression. In the current work, we searched for NTM-recognizing antibodies in specific cohorts of HIV-1 infected individuals, including long-term non-progressors (LTNP) and progressors. For this purpose, we employed a previously defined bioinformatics criterion for design of an NTM peptide mimetic to select an octapeptide, NTMs (FTDNAKTI), which is more suitable for use in a solid-state enzyme-linked immunosorbent assay (ELISA). Our results show that NTMs-reactive antibodies are significantly more prevalent (p LT 0.01) in LTNP as compared to progressors and healthy control subjects, indicating their association with non-progressive infection. The presence of antibodies recognizing the second conserved region of the HIV-1 gp120 derived peptide, NTMs, in LTNP sera suggest that these antibodies could be of considerable interest for development of anti-HIV immune-based therapies and vaccines.",
journal = "Current HIV Research",
title = "The presence of antibodies recognizing a peptide derived from the second conserved region of HIV-1 gp120 correlates with non-progressive HIV infection",
volume = "5",
number = "5",
pages = "443-448",
doi = "10.2174/157016207781662470"
}

Đorđević, A., Veljković, M., Antoni, S., Sakarellos-Daitsiotis, M., Krikorian, D., Zevgiti, S., Dietrich, U., Veljković, N. V.,& Branch, D. R.. (2007). The presence of antibodies recognizing a peptide derived from the second conserved region of HIV-1 gp120 correlates with non-progressive HIV infection. in Current HIV Research, 5(5), 443-448.
https://doi.org/10.2174/157016207781662470

Đorđević A, Veljković M, Antoni S, Sakarellos-Daitsiotis M, Krikorian D, Zevgiti S, Dietrich U, Veljković NV, Branch DR. The presence of antibodies recognizing a peptide derived from the second conserved region of HIV-1 gp120 correlates with non-progressive HIV infection. in Current HIV Research. 2007;5(5):443-448.
doi:10.2174/157016207781662470 .

Đorđević, Ana, Veljković, Milena, Antoni, Sascha, Sakarellos-Daitsiotis, Maria, Krikorian, Dimitrios, Zevgiti, Stella, Dietrich, Ursula, Veljković, Nevena V., Branch, Donald R., "The presence of antibodies recognizing a peptide derived from the second conserved region of HIV-1 gp120 correlates with non-progressive HIV infection" in Current HIV Research, 5, no. 5 (2007):443-448,
https://doi.org/10.2174/157016207781662470 . .

TY  - JOUR
AU  - Veljković, Veljko
AU  - Mouscadet, Jean-Francois
AU  - Veljković, Nevena V.
AU  - Glišić, Sanja
AU  - Debyser, Zeger
PY  - 2007
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3166
AB  - Flavonoid compounds represent an important natural source of antiretrovirals for AIDS therapy due to their significant anti-HIV-1 activity and low toxicity. Here we propose a simple theoretical criterion to discriminate active from inactive flavonoids that is suitable for rapid in silico screening of flavonoid libraries, and selection and optimization of lead compounds with anti-HIV-1 activity. (c) 2007 Elsevier Ltd. All rights reserved.
T2  - Bioorganic and Medicinal Chemistry Letters
T1  - Simple criterion for selection of flavonoid compounds with anti-HIV activity
VL  - 17
IS  - 5
SP  - 1226
EP  - 1232
DO  - 10.1016/j.bmcl.2006.12.029
ER  - 

@article{
author = "Veljković, Veljko and Mouscadet, Jean-Francois and Veljković, Nevena V. and Glišić, Sanja and Debyser, Zeger",
year = "2007",
abstract = "Flavonoid compounds represent an important natural source of antiretrovirals for AIDS therapy due to their significant anti-HIV-1 activity and low toxicity. Here we propose a simple theoretical criterion to discriminate active from inactive flavonoids that is suitable for rapid in silico screening of flavonoid libraries, and selection and optimization of lead compounds with anti-HIV-1 activity. (c) 2007 Elsevier Ltd. All rights reserved.",
journal = "Bioorganic and Medicinal Chemistry Letters",
title = "Simple criterion for selection of flavonoid compounds with anti-HIV activity",
volume = "17",
number = "5",
pages = "1226-1232",
doi = "10.1016/j.bmcl.2006.12.029"
}

Veljković, V., Mouscadet, J., Veljković, N. V., Glišić, S.,& Debyser, Z.. (2007). Simple criterion for selection of flavonoid compounds with anti-HIV activity. in Bioorganic and Medicinal Chemistry Letters, 17(5), 1226-1232.
https://doi.org/10.1016/j.bmcl.2006.12.029

Veljković V, Mouscadet J, Veljković NV, Glišić S, Debyser Z. Simple criterion for selection of flavonoid compounds with anti-HIV activity. in Bioorganic and Medicinal Chemistry Letters. 2007;17(5):1226-1232.
doi:10.1016/j.bmcl.2006.12.029 .

Veljković, Veljko, Mouscadet, Jean-Francois, Veljković, Nevena V., Glišić, Sanja, Debyser, Zeger, "Simple criterion for selection of flavonoid compounds with anti-HIV activity" in Bioorganic and Medicinal Chemistry Letters, 17, no. 5 (2007):1226-1232,
https://doi.org/10.1016/j.bmcl.2006.12.029 . .