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Carvalho, M. F., de Marco, P., Duque, A. F., Pacheco, C. C., et al. (2008). Labrys portucalensis sp. nov., a fluorobenzene-degrading bacterium isolated from an industrially contaminated sediment in northern Portugal. International Journal of Systematic and Evolutionary Microbiology, 58(3), 692 - 698.
Cardoso, M. S., Silva, T. M., Resende, M., Appelberg, R., & Borges, M. (2015). Lack of the transcription factor hypoxia-inducible factor 1α (HIF- 1α) in macrophages accelerates the necrosis of Mycobacterium avium-induced granulomas. Infection and Immunity, 83(9), 3534 - 3544.
Santos, S. G., Antoniou, A. N., Sampaio, P., Powis, S. J., & Arosa, F. A. (2006). Lack of tyrosine 320 impairs spontaneous endocytosis and enhances release of HLA-B27 molecules. Journal of Immunology, 176(5), 2942 - 2949.
Silva, T., Moreira, A. C., Nazmi, K., Moniz, T., et al. (2017). Lactoferricin peptides increase macrophages' capacity to kill Mycobacterium avium. mSphere, 2(4).
Oliveira, J., Santos, R., Soares-Silva, I., Jorge, P., et al. (2008). LAMA2 gene analysis in a cohort of 26 congenital muscular dystrophy patients. Clinical Genetics, 74(6), 502 - 512.
Vieira, L. M. M., Kijjoa, A., Silva, A. M. S., Mondranondra, I. - O., et al. (2004). Lanostanes and friedolanostanes from the bark of Garcinia speciosa. Phytochemistry, 65(4), 393 - 398.
Reis, O., Sousa, S., Camejo, A., Villiers, V., et al. (2010). LapB, a novel Listeria monocytogenes LPXTG surface adhesin, required for entry into eukaryotic cells and virulence. Journal of Infectious Diseases, 202(4), 551 - 562.
Sequeiros, J., Ramos, E. M., Cerqueira, J., Costa, M. C., et al. (2010). Large normal and reduced penetrance alleles in Huntington disease: Instability in families and frequency at the laboratory, at the clinic and in the population. Clinical Genetics, 78(4), 381 - 387.
van Meurs, J. B. J., Trikalinos, T. A., Ralston, S. H., Balcells, S., et al. (2008). Large-scale analysis of association between LRP5 and LRP6 variants and osteoporosis. JAMA - Journal of the American Medical Association, 299(11), 1277 - 1290.
Langdahl, B. L., Uitterlinden, A. G., Ralston, S. H., Trikalinos, T. A., et al. (2008). Large-scale analysis of association between polymorphisms in the transforming growth factor beta 1 gene (TGFB1) and osteoporosis: The GENOMOS study. Bone, 42(5), 969 - 981.
M. Pereira, daConceiçã, Morais, S., Sequeiros, J., & Alonso, I. (2016). Large-scale functional RNAi Screen in C. elegans identifies TGF-β and notch signaling pathways as modifiers of CACNAIA. ASN Neuro, 8(2).
Pinho, M. J., Cabral, J. M., Silva, E., Serrão, M. P., & Soares-Da-Silva, P. (2011). LAT1 overexpression and function compensates downregulation of ASCT2 in an in vitro model of renal proximal tubule cell ageing. Molecular and Cellular Biochemistry, 349(1-2), 107 - 116.
Afonso, O., Figueiredo, A. C., & Maiato, H. (2017). Late mitotic functions of Aurora kinases. Chromosoma, 126(1), 93 - 103.
Belo, L., Caslake, M., Santos-Silva, A., Castro, E. M. B., et al. (2004). LDL size, total antioxidant status and oxidised LDL in normal human pregnancy: A longitudinal study. Atherosclerosis, 177(2), 391 - 399.
Corral-Rodríguez, M. A., Macedo-Ribeiro, S., Barbosa Pereira, P. J., & Fuentes-Prior, P. (2010). Leech-derived thrombin inhibitors: From structures to mechanisms to clinical applications. Journal of Medicinal Chemistry, 53(10), 3847 - 3861.
Azevedo, O., Gaspar, P., Sá Miranda, C., Cunha, D., et al. (2011). Left ventricular noncompaction in a patient with Fabry disease: An unresolved challenge. Cardiology, 120(2), 97 - 99.
Azevedo, O., Gaspar, P., Sá Miranda, C., Cunha, D., et al. (2011). Left ventricular noncompaction in a patient with fabry disease: Overdiagnosis, morphological manifestation of fabry disease or two unrelated rare conditions in the same patient?. Cardiology, 119(3), 155 - 159.
Silvestre, R., Cordeiro-da-Silva, A., Tavares, J., Sereno, D., & Ouaissi, A. (2006). Leishmania cytosolic silent information regulatory protein 2 deacetylase induces murine B-cell differentiation and in vivo production of specific antibodies. Immunology, 119(4), 529 - 540.
Rodrigues, A., Claro, M., Alexandre-Pires, G., Santos-Mateus, D., et al. (2017). Leishmania infantum antigens modulate memory cell subsets of liver resident T lymphocyte. Immunobiology, 222(2), 409 - 422.
Faria, J., Loureiro, I., Santarém, N., Macedo-Ribeiro, S., et al. (2016). Leishmania infantum Asparagine Synthetase A Is Dispensable for Parasites Survival and Infectivity. PLoS Neglected Tropical Diseases, 10(1).
Tavares, J., Ouaissi, A., Santarém, N., Sereno, D., et al. (2008). The Leishmania infantum cytosolic SIR2-related protein 1 (LiSIR2RP1) is an NAD+-dependent deacetylase and ADP-ribosyltransferase. Biochemical Journal, 415(3), 377 - 386.
Menezes Cabral, S., Leal Silvestre, R., Moreira Santarém, N., Costa Tavares, J., et al. (2008). A Leishmania infantum cytosolic tryparedoxin activates B cells to secrete interleukin-10 and specific immunoglobulin. Immunology, 123(4), 555 - 565.
Rodrigues, A., Santos-Mateus, D., Alexandre-Pires, G., Valério-Bolas, A., et al. (2017). Leishmania infantum exerts immunomodulation in canine Kupffer cells reverted by meglumine antimoniate. Comparative Immunology, Microbiology and Infectious Diseases, 55, 42 - 52.
Belo, R., Santarém, N., Pereira, C., Pérez-Cabezas, B., et al. (2017). Leishmania infantum exoproducts inhibit human invariant NKT cell expansion and activation. Frontiers in Immunology, 8(JUN).
Moreira, D., Rodrigues, V., Abengozar, M., Rivas, L., et al. (2015). Leishmania infantum Modulates Host Macrophage Mitochondrial Metabolism by Hijacking the SIRT1-AMPK Axis. PLoS Pathogens, 11(3), 1 - 24.


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