All Outputs (78)

Quinolone resistance and ornithine decarboxylation activity in lactose-negative Escherichia coli (2015)
Journal Article
Gomig, F., Galvão, C. W., Freitas, D. L. D., Labas, L., Etto, R. M., Esmerino, L. A., Lima, M. A. D., Appel, M. H., Zanata, S. M., Steffens, M. B. R., Nader, H. B., & Silveira, R. B. D. (2015). Quinolone resistance and ornithine decarboxylation activity in lactose-negative Escherichia coli. Brazilian Journal of Microbiology, 46(3), 753-757. https://doi.org/10.1590/S1517-838246320131291

Quinolones and fluoroquinolones are widely used to treat uropathogenic Escherichia coli infections. Bacterial resistance to these antimicrobials primarily involves mutations in gyrA and parC genes. To date, no studies have examined the potential rela... Read More about Quinolone resistance and ornithine decarboxylation activity in lactose-negative Escherichia coli.

SULF2 overexpression positively regulates tumorigenicity of human prostate cancer cells (2015)
Journal Article
Vicente, C., Andrade De Lima, M., Nader, H., & Toma, L. (2015). SULF2 overexpression positively regulates tumorigenicity of human prostate cancer cells. Journal of Experimental & Clinical Cancer Research, 34, 25--25. https://doi.org/10.1186/s13046-015-0141-x

Background
SULF2 is a 6-O-endosulfatase which removes 6-O sulfate residues from N-glucosamine present on heparan sulfate (HS). The sulfation pattern of HS influences signaling events mediated by heparan sulfate proteoglycans (HSPGs) located on cell... Read More about SULF2 overexpression positively regulates tumorigenicity of human prostate cancer cells.

Heparan sulfate and heparin interactions with proteins (2015)
Journal Article
Meneghetti, M., Hughes, A., Rudd, T., Nader, H., Powell, A., Yates, E., & Lima, M. (2015). Heparan sulfate and heparin interactions with proteins. Journal of the Royal Society. Interface, 12, 20150589--20150589. https://doi.org/10.1098/rsif.2015.0589

Development of new methods for determining the heparanase enzymatic activity (2015)
Journal Article
Melo, C., Tersariol, I., Nader, H., Pinhal, M., & Lima, M. (2015). Development of new methods for determining the heparanase enzymatic activity. Carbohydrate Research, 412, 66--70. https://doi.org/10.1016/j.carres.2015.04.020

From Combinatorial Display Techniques to Microarray Technology: New Approaches to the Development and Toxicological Profiling of Targeted Nanomedicines (2014)
Book Chapter
Justo, G., Suarez, E., Melo, C., Lima, M., Nader, H., & Pinhal, M. (2014). From Combinatorial Display Techniques to Microarray Technology: New Approaches to the Development and Toxicological Profiling of Targeted Nanomedicines. In Nanotoxicology (153--175). Springer, New York, NY

Unfractionated and low molecular weight heparin (2014)
Presentation / Conference Contribution
Lima, M., & Nader, H. Unfractionated and low molecular weight heparin

A heparin-like glycosaminoglycan from shrimp containing high levels of 3-O-sulfated D-glucosamine groups in an unusual trisaccharide sequence (2014)
Journal Article
Chavante, S., Brito, A., Lima, M., Yates, E., Nader, H., Guerrini, M., Torri, G., & Bisio, A. (2014). A heparin-like glycosaminoglycan from shrimp containing high levels of 3-O-sulfated D-glucosamine groups in an unusual trisaccharide sequence. Carbohydrate Research, 390, 59--66. https://doi.org/10.1016/j.carres.2014.03.002

Ultra-low-molecular-weight heparins: Precise structural features impacting specific anticoagulant activities (2013)
Journal Article
Lima, M., Viskov, C., Herman, F., Gray, A., de Farias, E., Cavalheiro, R., Sassaki, G., Hoppensteadt, D., Fareed, F., & Nader, H. (2013). Ultra-low-molecular-weight heparins: Precise structural features impacting specific anticoagulant activities. Thrombosis and Haemostasis, 109(03), 471-478. https://doi.org/10.1160/TH12-11-0795

Ultra-low-molecular-weight heparins (ULMWHs) with better efficacy and safety ratios are under development; however, there are few structural data available. The main structural features and molecular weight of ULMWHs were studied and compared to enox... Read More about Ultra-low-molecular-weight heparins: Precise structural features impacting specific anticoagulant activities.

On the catalytic mechanism of polysaccharide lyases: evidence of His and Tyr involvement in heparin lysis by heparinase I and the role of Ca2+ (2013)
Journal Article
Córdula, C. R., Lima, M. A., Shinjo, S. K., Gesteira, T. F., Pol-Fachin, L., Coulson-Thomas, V. J., Verli, H., Yates, E. A., Rudd, T. R., Pinhal, M. A. S., Toma, L., Dietrich, C. P., Nader, H. B., & Tersariol, I. L. S. (2013). On the catalytic mechanism of polysaccharide lyases: evidence of His and Tyr involvement in heparin lysis by heparinase I and the role of Ca2+. Molecular BioSystems, 10(1), 54-64. https://doi.org/10.1039/C3MB70370C

The structurally diverse polysaccharide lyase enzymes are distributed from plants to animals but share common catalytic mechanisms. One, heparinase I (F. heparinum), is employed in the production of the major anticoagulant drug, low molecular weight... Read More about On the catalytic mechanism of polysaccharide lyases: evidence of His and Tyr involvement in heparin lysis by heparinase I and the role of Ca2+.

A heparin-like compound isolated from a marine crab rich in glucuronic acid 2-O-sulfate presents low anticoagulant activity (2013)
Journal Article
Andrade, G., Lima, M., de Souza Junior, A., Fareed, J., Hoppensteadt, D., Santos, E., Chavante, S., Oliveira, F., Rocha, H., & Nader, H. (2013). A heparin-like compound isolated from a marine crab rich in glucuronic acid 2-O-sulfate presents low anticoagulant activity. Carbohydrate Polymers, 94, 647--654. https://doi.org/10.1016/j.carbpol.2013.01.069

A non-hemorrhagic hybrid heparin/heparan sulfate with anticoagulant potential (2013)
Journal Article
Brito, A., Cavalcante, R., Palhares, L., Hughes, A., Andrade, G., Yates, E., Nader, H., Lima, M., & Chavante, S. (2013). A non-hemorrhagic hybrid heparin/heparan sulfate with anticoagulant potential. Carbohydrate Polymers, 99, 372--378. https://doi.org/10.1016/j.carbpol.2013.08.063

Insights into the N-sulfation mechanism: molecular dynamics simulations of the N-sulfotransferase domain of NDST1 and mutants (2013)
Journal Article
Gesteira, T., Pol-Fachin, L., Coulson-Thomas, V., Lima, M., Verli, H., & Nader, H. (2013). Insights into the N-sulfation mechanism: molecular dynamics simulations of the N-sulfotransferase domain of NDST1 and mutants. PloS one, 8, e70880--e70880. https://doi.org/10.1371/journal.pone.0070880

Antithrombin stabilisation by sulfated carbohydrates correlates with anticoagulant activity (2013)
Journal Article
Lima, M., Hughes, A. J., Veraldi, N., Rudd, T. R., Hussain, R., Brito, A. S., Chavante, S. F., Tersariol, I. I., Siligardi, G., Nader, H. B., & Yates, E. A. (2013). Antithrombin stabilisation by sulfated carbohydrates correlates with anticoagulant activity. MedChemComm, 4, 870--873. https://doi.org/10.1039/C3MD00048F

Glycosaminoglycan backbone is not required for the modulation of hemostasis: Effect of different heparin derivatives and non-glycosaminoglycan analogs (2012)
Journal Article
Bouças, R., Jarrouge-Bouças, T., Lima, M., Trindade, E., Moraes, F., Cavalheiro, R., Tersariol, I., Hoppenstead, D., Fareed, J., & Nader, H. (2012). Glycosaminoglycan backbone is not required for the modulation of hemostasis: Effect of different heparin derivatives and non-glycosaminoglycan analogs. Matrix Biology, 31, 308--316. https://doi.org/10.1016/j.matbio.2012.03.001

Structural and pharmacological profile of generic enoxaparins used in Brazil (2012)
Journal Article
Lima, M., de Farias, E., Gray, A., Sadeghi, N., Gesteira, T., Cavalheiro, R., Hoppensteadt, D., Fareed, J., Sassaki, G., & Nader, H. (2012). Structural and pharmacological profile of generic enoxaparins used in Brazil. Clinical and Applied Thrombosis/Hemostasis, 18, 379--386. https://doi.org/10.1177/1076029611426870

Lepstospira interrogans shotgun phage display identified LigB as a heparin-binding protein (2012)
Journal Article
Ching, A., Fávaro, R., Lima, S., Chaves, A., de Lima, M., Nader, H., Abreu, P., & Ho, P. (2012). Lepstospira interrogans shotgun phage display identified LigB as a heparin-binding protein. Biochemical and Biophysical Research Communications, 427, 774--779. https://doi.org/10.1016/j.bbrc.2012.09.137

The 2019 coronavirus (SARS-CoV-2) surface protein (Spike) S1 Receptor Binding Domain undergoes conformational change upon heparin binding
Journal Article
Mycroft-West, C., Su, D., Elli, S., Li, Y., Guimond, S., Miller, G., Turnbull, J., Yates, E., Guerrini, M., Fernig, D., Lima, M., & Skidmore, M. (2020). The 2019 coronavirus (SARS-CoV-2) surface protein (Spike) S1 Receptor Binding Domain undergoes conformational change upon heparin binding. arXiv, https://doi.org/10.1101/2020.02.29.971093

Many pathogens take advantage of the dependence of the host on the interaction of hundreds of extracellular proteins with the glycosaminoglycans heparan sulphate to regulate homeostasis and use heparan sulphate as a means to adhere and gain access to... Read More about The 2019 coronavirus (SARS-CoV-2) surface protein (Spike) S1 Receptor Binding Domain undergoes conformational change upon heparin binding.

Heparin inhibits cellular invasion by SARS-CoV-2: structural dependence of the interaction of the surface protein (spike) S1 receptor binding domain with heparin
Other
Mycroft-West, C. J., Su, D., Pagani, I., Rudd, T. R., Elli, S., Guimond, S. E., Miller, G., Meneghetti, M. C. Z., Nader, H. B., Li, Y., Nunes, Q. M., Procter, P., Mancini, N., Clementi, M., Bisio, A., Forsyth, N. R., Turnbull, J. E., Guerrini, M., Fernig, D. G., Vicenzi, E., …Skidmore, M. A. Heparin inhibits cellular invasion by SARS-CoV-2: structural dependence of the interaction of the surface protein (spike) S1 receptor binding domain with heparin