TY  - JOUR
AU  - Pompach, Petr
AU  - Viola, Cristina M.
AU  - Radosavljević, Jelena
AU  - Lin, Jingjing
AU  - Jiráček, Jirˇí
AU  - Brzozowski, Andrzej M.
AU  - Selicharová, Irena
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3719
AB  - Structural details of changes accompanying interaction between insulin-related hormones and their binding partners are often enigmatic. Here, cross-linking/mass spectrometry could complement structural techniques and reveal details of these protein-protein interfaces. We used such approach to clarify missing structural description of the interface in human insulin-like growth factor (IGF-1): Drosophila melanogaster imaginal morphogenesis protein-late 2 protein (Imp-L2) complex which we studied previously by X-ray crystallography. We crosslinked these proteins by heterobifunctional cross-linker sulfosuccinimidyl 4,4′-azidopentanoate (Sulfo-SDA) for the subsequent mass spectrometry (MS) analysis. The MS analysis revealed IGF-1:Imp-L2 interactions which were not resolved in the crystal structure of this assembly, and they converged with X-ray results, indicating the importance of the IGF-1 N-terminus interaction with the C-terminal (185–242) part of the Imp-L2 for stability of this complex. Here, we also showed the advantage and reliability of MS approach in solving details of protein-protein interactions that are too flexible for solid state structural methods.
PB  - Frontiers Media S.A.
T2  - Frontiers in Endocrinology
T1  - Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2
VL  - 10
DO  - 10.3389/fendo.2019.00695
ER  - 

@article{
author = "Pompach, Petr and Viola, Cristina M. and Radosavljević, Jelena and Lin, Jingjing and Jiráček, Jirˇí and Brzozowski, Andrzej M. and Selicharová, Irena",
year = "2019",
abstract = "Structural details of changes accompanying interaction between insulin-related hormones and their binding partners are often enigmatic. Here, cross-linking/mass spectrometry could complement structural techniques and reveal details of these protein-protein interfaces. We used such approach to clarify missing structural description of the interface in human insulin-like growth factor (IGF-1): Drosophila melanogaster imaginal morphogenesis protein-late 2 protein (Imp-L2) complex which we studied previously by X-ray crystallography. We crosslinked these proteins by heterobifunctional cross-linker sulfosuccinimidyl 4,4′-azidopentanoate (Sulfo-SDA) for the subsequent mass spectrometry (MS) analysis. The MS analysis revealed IGF-1:Imp-L2 interactions which were not resolved in the crystal structure of this assembly, and they converged with X-ray results, indicating the importance of the IGF-1 N-terminus interaction with the C-terminal (185–242) part of the Imp-L2 for stability of this complex. Here, we also showed the advantage and reliability of MS approach in solving details of protein-protein interactions that are too flexible for solid state structural methods.",
publisher = "Frontiers Media S.A.",
journal = "Frontiers in Endocrinology",
title = "Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2",
volume = "10",
doi = "10.3389/fendo.2019.00695"
}

Pompach, P., Viola, C. M., Radosavljević, J., Lin, J., Jiráček, J., Brzozowski, A. M.,& Selicharová, I.. (2019). Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2. in Frontiers in Endocrinology
Frontiers Media S.A.., 10.
https://doi.org/10.3389/fendo.2019.00695

Pompach P, Viola CM, Radosavljević J, Lin J, Jiráček J, Brzozowski AM, Selicharová I. Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2. in Frontiers in Endocrinology. 2019;10.
doi:10.3389/fendo.2019.00695 .

Pompach, Petr, Viola, Cristina M., Radosavljević, Jelena, Lin, Jingjing, Jiráček, Jirˇí, Brzozowski, Andrzej M., Selicharová, Irena, "Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2" in Frontiers in Endocrinology, 10 (2019),
https://doi.org/10.3389/fendo.2019.00695 . .

TY  - DATA
AU  - Pompach, Petr
AU  - Viola, Cristina M.
AU  - Radosavljević, Jelena
AU  - Lin, Jingjing
AU  - Jiráček, Jirˇí
AU  - Brzozowski, Andrzej M.
AU  - Selicharová, Irena
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3720
PB  - Frontiers Media S.A.
T2  - Frontiers in Endocrinology
T1  - Supplementary data for the article: Pompach, P.; Viola, C. M.; Radosavljević, J.; Lin, J.; Jiráček, J.; Brzozowski, A. M.; Selicharová, I. Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2. Frontiers in Endocrinology 2019, 10. https://doi.org/10.3389/fendo.2019.00695
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3720
ER  - 

@misc{
author = "Pompach, Petr and Viola, Cristina M. and Radosavljević, Jelena and Lin, Jingjing and Jiráček, Jirˇí and Brzozowski, Andrzej M. and Selicharová, Irena",
year = "2019",
publisher = "Frontiers Media S.A.",
journal = "Frontiers in Endocrinology",
title = "Supplementary data for the article: Pompach, P.; Viola, C. M.; Radosavljević, J.; Lin, J.; Jiráček, J.; Brzozowski, A. M.; Selicharová, I. Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2. Frontiers in Endocrinology 2019, 10. https://doi.org/10.3389/fendo.2019.00695",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3720"
}

Pompach, P., Viola, C. M., Radosavljević, J., Lin, J., Jiráček, J., Brzozowski, A. M.,& Selicharová, I.. (2019). Supplementary data for the article: Pompach, P.; Viola, C. M.; Radosavljević, J.; Lin, J.; Jiráček, J.; Brzozowski, A. M.; Selicharová, I. Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2. Frontiers in Endocrinology 2019, 10. https://doi.org/10.3389/fendo.2019.00695. in Frontiers in Endocrinology
Frontiers Media S.A...
https://hdl.handle.net/21.15107/rcub_cherry_3720

Pompach P, Viola CM, Radosavljević J, Lin J, Jiráček J, Brzozowski AM, Selicharová I. Supplementary data for the article: Pompach, P.; Viola, C. M.; Radosavljević, J.; Lin, J.; Jiráček, J.; Brzozowski, A. M.; Selicharová, I. Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2. Frontiers in Endocrinology 2019, 10. https://doi.org/10.3389/fendo.2019.00695. in Frontiers in Endocrinology. 2019;.
https://hdl.handle.net/21.15107/rcub_cherry_3720 .

Pompach, Petr, Viola, Cristina M., Radosavljević, Jelena, Lin, Jingjing, Jiráček, Jirˇí, Brzozowski, Andrzej M., Selicharová, Irena, "Supplementary data for the article: Pompach, P.; Viola, C. M.; Radosavljević, J.; Lin, J.; Jiráček, J.; Brzozowski, A. M.; Selicharová, I. Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2. Frontiers in Endocrinology 2019, 10. https://doi.org/10.3389/fendo.2019.00695" in Frontiers in Endocrinology (2019),
https://hdl.handle.net/21.15107/rcub_cherry_3720 .

TY  - JOUR
AU  - Machackova, Katerina
AU  - Chrudinova, Martina
AU  - Radosavljević, Jelena
AU  - Potalitsyn, Paulo
AU  - Krizkova, Kvetoslava
AU  - Fabry, Milan
AU  - Selicharova, Irena
AU  - Collinsova, Michaela
AU  - Brzozowski, Andrzej M.
AU  - Zakova, Lenka
AU  - Jiracek, Jiri
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2135
AB  - Insulin-like growth factors 1 and 2 (IGF-1 and -2, respectively) are protein hormones involved not only in normal growth and development but also in life span regulation and cancer. They exert their functions mainly through the IGF-1R or by binding to isoform A of the insulin receptor (IR-A). The development of IGF-1 and IGF-2 antagonists is of great clinical interest. Mutations of A4 and A8 sites of human insulin lead to disproportionate effects on hormone IR binding and activation. Here, we systematically modified IGF-1 sites 45, 46, and 49 and IGF-2 sites 45 and 48, which correspond, or are close, to insulin sites A4 and A8. The IGF-1R and IR-A binding and autophosphorylation potencies of these analogues were characterized. They retained the main IGF-1R-related properties, but the hormones with His49 in IGF-1 and His48 in IGF-2 showed significantly higher affinities for IR-A and for IR-B, being the strongest IGF-1- and IGF-2-like binders of these receptors ever reported. All analogues activated IR-A and IGF-1R without major discrepancies in their binding affinities. This study revealed that IR-A and IGF-1R contain specific sites, likely parts of their so-called sites 2', which can interact differently with specifically modified IGF analogues. Moreover, a clear importance of IGF-2 site 44 for effective hormone folding was also observed. These findings may facilitate novel and rational engineering of new hormone analogues for IR-A and IGF-1R studies and for potential medical applications.
PB  - Amer Chemical Soc, Washington
T2  - Biochemistry
T1  - Converting Insulin-like Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the Introduction of an Evolutionarily Divergent Mutation
VL  - 57
IS  - 16
SP  - 2373
EP  - 2382
DO  - 10.1021/acs.biochem.7b01260
ER  - 

@article{
author = "Machackova, Katerina and Chrudinova, Martina and Radosavljević, Jelena and Potalitsyn, Paulo and Krizkova, Kvetoslava and Fabry, Milan and Selicharova, Irena and Collinsova, Michaela and Brzozowski, Andrzej M. and Zakova, Lenka and Jiracek, Jiri",
year = "2018",
abstract = "Insulin-like growth factors 1 and 2 (IGF-1 and -2, respectively) are protein hormones involved not only in normal growth and development but also in life span regulation and cancer. They exert their functions mainly through the IGF-1R or by binding to isoform A of the insulin receptor (IR-A). The development of IGF-1 and IGF-2 antagonists is of great clinical interest. Mutations of A4 and A8 sites of human insulin lead to disproportionate effects on hormone IR binding and activation. Here, we systematically modified IGF-1 sites 45, 46, and 49 and IGF-2 sites 45 and 48, which correspond, or are close, to insulin sites A4 and A8. The IGF-1R and IR-A binding and autophosphorylation potencies of these analogues were characterized. They retained the main IGF-1R-related properties, but the hormones with His49 in IGF-1 and His48 in IGF-2 showed significantly higher affinities for IR-A and for IR-B, being the strongest IGF-1- and IGF-2-like binders of these receptors ever reported. All analogues activated IR-A and IGF-1R without major discrepancies in their binding affinities. This study revealed that IR-A and IGF-1R contain specific sites, likely parts of their so-called sites 2', which can interact differently with specifically modified IGF analogues. Moreover, a clear importance of IGF-2 site 44 for effective hormone folding was also observed. These findings may facilitate novel and rational engineering of new hormone analogues for IR-A and IGF-1R studies and for potential medical applications.",
publisher = "Amer Chemical Soc, Washington",
journal = "Biochemistry",
title = "Converting Insulin-like Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the Introduction of an Evolutionarily Divergent Mutation",
volume = "57",
number = "16",
pages = "2373-2382",
doi = "10.1021/acs.biochem.7b01260"
}

Machackova, K., Chrudinova, M., Radosavljević, J., Potalitsyn, P., Krizkova, K., Fabry, M., Selicharova, I., Collinsova, M., Brzozowski, A. M., Zakova, L.,& Jiracek, J.. (2018). Converting Insulin-like Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the Introduction of an Evolutionarily Divergent Mutation. in Biochemistry
Amer Chemical Soc, Washington., 57(16), 2373-2382.
https://doi.org/10.1021/acs.biochem.7b01260

Machackova K, Chrudinova M, Radosavljević J, Potalitsyn P, Krizkova K, Fabry M, Selicharova I, Collinsova M, Brzozowski AM, Zakova L, Jiracek J. Converting Insulin-like Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the Introduction of an Evolutionarily Divergent Mutation. in Biochemistry. 2018;57(16):2373-2382.
doi:10.1021/acs.biochem.7b01260 .

Machackova, Katerina, Chrudinova, Martina, Radosavljević, Jelena, Potalitsyn, Paulo, Krizkova, Kvetoslava, Fabry, Milan, Selicharova, Irena, Collinsova, Michaela, Brzozowski, Andrzej M., Zakova, Lenka, Jiracek, Jiri, "Converting Insulin-like Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the Introduction of an Evolutionarily Divergent Mutation" in Biochemistry, 57, no. 16 (2018):2373-2382,
https://doi.org/10.1021/acs.biochem.7b01260 . .

TY  - DATA
AU  - Machackova, Katerina
AU  - Chrudinova, Martina
AU  - Radosavljević, Jelena
AU  - Potalitsyn, Paulo
AU  - Krizkova, Kvetoslava
AU  - Fabry, Milan
AU  - Selicharova, Irena
AU  - Collinsova, Michaela
AU  - Brzozowski, Andrzej M.
AU  - Zakova, Lenka
AU  - Jiracek, Jiri
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3185
PB  - Amer Chemical Soc, Washington
T2  - Biochemistry
T1  - Supplementary material for the article: Macháčková, K.; Chrudinová, M.; Radosavljević, J.; Potalitsyn, P.; Křížková, K.; Fábry, M.;  Selicharová, I.; Collinsová, M.; Brzozowski, A. M.; Žáková, L.; et al. Converting Insulin-like  Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the  Introduction of an Evolutionarily Divergent Mutation. Biochemistry 2018, 57 (16), 2373– 2382. https://doi.org/10.1021/acs.biochem.7b01260
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3185
ER  - 

@misc{
author = "Machackova, Katerina and Chrudinova, Martina and Radosavljević, Jelena and Potalitsyn, Paulo and Krizkova, Kvetoslava and Fabry, Milan and Selicharova, Irena and Collinsova, Michaela and Brzozowski, Andrzej M. and Zakova, Lenka and Jiracek, Jiri",
year = "2018",
publisher = "Amer Chemical Soc, Washington",
journal = "Biochemistry",
title = "Supplementary material for the article: Macháčková, K.; Chrudinová, M.; Radosavljević, J.; Potalitsyn, P.; Křížková, K.; Fábry, M.;  Selicharová, I.; Collinsová, M.; Brzozowski, A. M.; Žáková, L.; et al. Converting Insulin-like  Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the  Introduction of an Evolutionarily Divergent Mutation. Biochemistry 2018, 57 (16), 2373– 2382. https://doi.org/10.1021/acs.biochem.7b01260",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3185"
}

Machackova, K., Chrudinova, M., Radosavljević, J., Potalitsyn, P., Krizkova, K., Fabry, M., Selicharova, I., Collinsova, M., Brzozowski, A. M., Zakova, L.,& Jiracek, J.. (2018). Supplementary material for the article: Macháčková, K.; Chrudinová, M.; Radosavljević, J.; Potalitsyn, P.; Křížková, K.; Fábry, M.;  Selicharová, I.; Collinsová, M.; Brzozowski, A. M.; Žáková, L.; et al. Converting Insulin-like  Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the  Introduction of an Evolutionarily Divergent Mutation. Biochemistry 2018, 57 (16), 2373– 2382. https://doi.org/10.1021/acs.biochem.7b01260. in Biochemistry
Amer Chemical Soc, Washington..
https://hdl.handle.net/21.15107/rcub_cherry_3185

Machackova K, Chrudinova M, Radosavljević J, Potalitsyn P, Krizkova K, Fabry M, Selicharova I, Collinsova M, Brzozowski AM, Zakova L, Jiracek J. Supplementary material for the article: Macháčková, K.; Chrudinová, M.; Radosavljević, J.; Potalitsyn, P.; Křížková, K.; Fábry, M.;  Selicharová, I.; Collinsová, M.; Brzozowski, A. M.; Žáková, L.; et al. Converting Insulin-like  Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the  Introduction of an Evolutionarily Divergent Mutation. Biochemistry 2018, 57 (16), 2373– 2382. https://doi.org/10.1021/acs.biochem.7b01260. in Biochemistry. 2018;.
https://hdl.handle.net/21.15107/rcub_cherry_3185 .

Machackova, Katerina, Chrudinova, Martina, Radosavljević, Jelena, Potalitsyn, Paulo, Krizkova, Kvetoslava, Fabry, Milan, Selicharova, Irena, Collinsova, Michaela, Brzozowski, Andrzej M., Zakova, Lenka, Jiracek, Jiri, "Supplementary material for the article: Macháčková, K.; Chrudinová, M.; Radosavljević, J.; Potalitsyn, P.; Křížková, K.; Fábry, M.;  Selicharová, I.; Collinsová, M.; Brzozowski, A. M.; Žáková, L.; et al. Converting Insulin-like  Growth Factors 1 and 2 into High-Affinity Ligands for Insulin Receptor Isoform A by the  Introduction of an Evolutionarily Divergent Mutation. Biochemistry 2018, 57 (16), 2373– 2382. https://doi.org/10.1021/acs.biochem.7b01260" in Biochemistry (2018),
https://hdl.handle.net/21.15107/rcub_cherry_3185 .