Identificação pessoal

Nome completo

Ana Barbas

Nomes de citação

• Barbas, Ana

Identificadores de autor

Ciência ID

711F-FAE7-E21E

ORCID iD

0000-0002-6245-8549

Telefones

Telefone

• 214469441 (Profissional)

Moradas

• iBET, Avenida da Republica, EAN, 2781-901, Oeiras, Oeiras, Portugal (Profissional)

Websites

• https://www.linkedin.com/in/ana-barbas-356375b/ (Rede social)

Domínios de atuação

• Ciências Médicas e da Saúde - Biotecnologia Médica - Biotecnologia Aplicada à Saúde

Idiomas

Idioma	Conversação	Leitura	Escrita	Compreensão	Peer-review
Português (Idioma materno)
Inglês	Utilizador proficiente (C2)	Utilizador proficiente (C2)	Utilizador proficiente (C2)	Utilizador proficiente (C2)	Utilizador proficiente (C2)
Alemão	Utilizador independente (B1)	Utilizador independente (B1)	Utilizador independente (B1)	Utilizador independente (B1)	Utilizador independente (B1)
Francês	Utilizador elementar (A2)	Utilizador elementar (A2)	Utilizador elementar (A2)	Utilizador elementar (A2)	Utilizador elementar (A2)

	Grau	Classificação
2008/01/01 - 2009/10/01 Concluído	Ciências da Engenharia e Tecnologia (Pós-doutoramento) Especialização em Biotecnologia Universidade Nova de Lisboa Instituto de Tecnologia Química e Biológica, Portugal	n/a
2003/09/01 - 2007/12/14 Concluído	Ciências e Engenharias Químicas e Biológicas (Doutoramento) Especialização em Ciência Biológicas Universidade Nova de Lisboa Instituto de Tecnologia Química e Biológica, Portugal "Functional and Structural Studies on Escherichia coli RNase II: a crucial enzyme in RNA metabolism. " (TESE/DISSERTAÇÃO)	unanimidade
1994/09/15 - 1999/07/15 Concluído	Química Aplicada (Licenciatura) Especialização em Biotecnologia Universidade Nova de Lisboa Faculdade de Ciências e Tecnologia, Portugal "Production of Recombinant Cytokines in Escherichia coli - Case study of interferon alha" (TESE/DISSERTAÇÃO)	15

Ciência

	Categoria Profissional Instituição de acolhimento	Empregador
2015/01/01 - Atual	Investigador Contratado (Investigação)	Bayer Portugal SA, Portugal
	Bayer Portugal SA, Portugal (...)
2009/11/01 - 2014/12/31	Investigador (Investigação)	Instituto de Biologia Experimental e Tecnológica, Portugal
	Instituto de Biologia Experimental e Tecnológica, Portugal
1999/09/15 - 2003/07/15	Investigador (Investigação)	Biotecnol SA, Portugal
	Universidade Nova de Lisboa Instituto de Tecnologia Química e Biológica, Portugal

Bolsa

	Designação	Financiadores
2013/07 - 2015/12	Combining siRNA and AAV therapy approaches to target human basal-like breast cancer: from vector development to anti-tumor efficacy evaluation. Provided by PTCRIS: 126222	Universidade de Coimbra
2012/03 - 2015/09	Viral Capture and Purification System: Smart macroporous structures for the affinity purification of retroviral particles Provided by PTCRIS: 118317	Universidade de Coimbra
2012/03 - 2015/09	Development of function blocking antibodies using Phage Display Technology: Inhibiton of the Notch1 signaling pathway by function blocking anti-jagged 1 antibody. Provided by PTCRIS: 121670	Universidade de Coimbra
2013/07 - 2014/09	Development of a scalable strategy for stem cells purification Provided by PTCRIS: 128543	Universidade de Coimbra
2008/01 - 2011/03	Elucidating the Critical Role of RNase II family of Enzymes in RNA metabolism: Structural and Functional Studies Provided by PTCRIS: 71453	Universidade de Coimbra
2008/01 - 2011/03	Biochemical and Structural Studies of UDP-Glucose Dehydrogenases Provided by PTCRIS: 67925	Universidade de Coimbra
2007/11 - 2011/03	RNase II-like enzymes and non-coding RNAs and their role in the pathogenicity of Streptococcus pneumoniae Provided by PTCRIS: 71454	Universidade de Coimbra
2007/01 - 2009/06	The role of small non-coding RNAs and RNases on the pathogenicity of Salmonella. Provided by PTCRIS: 82542	Universidade de Coimbra
2007/01 - 2009/03	The role of RNase R and its Homologues in the Control of Gene Expression:Structural and Functional Studies Provided by PTCRIS: 82015 Provided by PTCRIS: 55106	Universidade de Coimbra
2005/09 - 2008/02	The role of small non-coding RNAs and RNases on the pathogenicity of Salmonella. Provided by PTCRIS: 56811	Fundação para a Ciência e a Tecnologia

Publicações

Artigo em revista

Catarina Pinto; Gabriela Silva; Ana S. Ribeiro; Mónica Oliveira; Manuel Garrido; Vanessa S. Bandeira; André Nascimento; et al. "Evaluation of AAV-mediated delivery of shRNA to target basal-like breast cancer genetic vulnerabilities". Journal of Biotechnology 300 (2019): 70-77. https://doi.org/10.1016/j.jbiotec.2019.05.016. 10.1016/j.jbiotec.2019.05.016 Sales-Dias J; Silva G; Lamy M; Ferreira A; Barbas A. "The Notch ligand DLL1 exerts carcinogenic features in human breast cancer cells.". PloS one (2019): http://europepmc.org/abstract/med/31107884. 10.1371/journal.pone.0217002 Ferreira A; Lamy M; Margarida Rocha M; Silva G; Bandeiras TM; Barbas A. "Production and characterization of a novel Delta-like 1 functional unit as a tool for Notch pathway activation and generation of a specific antibody.". Protein expression and purification (2018): http://europepmc.org/abstract/med/29366964. 10.1016/j.pep.2018.01.008 Loureiro, L.R.; Sousa, D.P.; Ferreira, D.; Chai, W.; Lima, L.; Pereira, C.; Lopes, C.B.; et al. "Novel monoclonal antibody L2A5 specifically targeting sialyl-Tn and short glycans terminated by alpha-2–6 sialic acids". Scientific Reports 8 1 (2018): http://www.scopus.com/inward/record.url?eid=2-s2.0-85051658578&partnerID=MN8TOARS. 10.1038/s41598-018-30421-w Goncalves, J.; Santos, M.; Acurcio, R.; Iria, I.; Gouveia, L.; Matos Brito, P.; Catarina Cunha-Santos, A.; et al. "Antigenic response to CT-P13 and infliximab originator in inflammatory bowel disease patients shows similar epitope recognition". Alimentary Pharmacology and Therapeutics 48 5 (2018): 507-522. http://www.scopus.com/inward/record.url?eid=2-s2.0-85051269231&partnerID=MN8TOARS. 10.1111/apt.14808 Lamy, M.; Ferreira, A.; Dias, J.S.; Braga, S.; Silva, G.; Barbas, A.. "Notch-out for breast cancer therapies". New Biotechnology 39 (2017): 215-221. http://www.scopus.com/inward/record.url?eid=2-s2.0-85028763617&partnerID=MN8TOARS. 10.1016/j.nbt.2017.08.004 Fernandes, C.S.M.; Barbosa, I.; Castro, R.; Pina, A.S.; Coroadinha, A.S.; Barbas, A.; Roque, A.C.A.. "Retroviral particles are effectively purified on an affinity matrix containing peptides selected by phage-display". Biotechnology Journal 11 12 (2016): 1513-1524. http://www.scopus.com/inward/record.url?eid=2-s2.0-84995387896&partnerID=MN8TOARS. 10.1002/biot.201600025 Loureiro, L.R.; Carrascal, M.A.; Barbas, A.; Ramalho, J.S.; Novo, C.; Delannoy, P.; Videira, P.A.. "Challenges in antibody development against Tn and sialyl-Tn antigens". Biomolecules 5 3 (2015): 1783-1809. http://www.scopus.com/inward/record.url?eid=2-s2.0-85012077616&partnerID=MN8TOARS. 10.3390/biom5031783 Reis, F.P.; Barbas, A.; Klauer-King, A.A.; Tsanova, B.; Schaeffer, D.; López-Viñas, E.; Gómez-Puertas, P.; Van Hoof, A.; Arraiano, C.M.. "Erratum: Correction: Modulating the RNA Processing and Decay by the Exosome: Altering Rrp44/Dis3 Activity and End-Product (PLoS ONE (2015) 10:8 (e0136810) (doi:10.1371/journal.pone.0136810))". PLoS ONE 10 8 (2015): http://www.scopus.com/inward/record.url?eid=2-s2.0-84942852941&partnerID=MN8TOARS. 10.1371/journal.pone.0136810 Reis, F.P.; Barbas, A.; Klauer-King, A.A.; Tsanova, B.; Schaeffer, D.; López-Viñas, E.; Gómez-Puertas, P.; Van Hoof, A.; Arraiano, C.M.. "Modulating the RNA processing and decay by the exosome: Altering Rrp44/Dis3 activity and end-product". PLoS ONE 8 11 (2013): http://www.scopus.com/inward/record.url?eid=2-s2.0-84893157627&partnerID=MN8TOARS. 10.1371/journal.pone.0076504 Barbas, A.; Popescu, A.; Frazão, C.; Arraiano, C.M.; Fialho, A.M.. "Rossmann-fold motifs can confer multiple functions to metabolic enzymes: RNA binding and ribonuclease activity of a UDP-glucose dehydrogenase". Biochemical and Biophysical Research Communications 430 1 (2013): 218-224. http://www.scopus.com/inward/record.url?eid=2-s2.0-84872422260&partnerID=MN8TOARS. 10.1016/j.bbrc.2012.10.091 Matos, R.G.; Barbas, A.; Gómez-Puertas, P.; Arraiano, C.M.. "Swapping the domains of exoribonucleases RNase II and RNase R: Conferring upon RNase II the ability to degrade ds RNA". Proteins: Structure, Function and Bioinformatics 79 6 (2011): 1853-1867. http://www.scopus.com/inward/record.url?eid=2-s2.0-79955713801&partnerID=MN8TOARS. 10.1002/prot.23010 Arraiano, C.M.; Matos, R.G.; Barbas, A.. "RNase II: The finer details of the modus operandi of a molecular killer". RNA Biology 7 3 (2010): http://www.scopus.com/inward/record.url?eid=2-s2.0-85011942110&partnerID=MN8TOARS. Matos, R.G.; Barbas, A.; Arraiano, C.M.. "Comparison of EMSA and SPR for the characterization of RNA-RNase II complexes". Protein Journal 29 6 (2010): 394-397. http://www.scopus.com/inward/record.url?eid=2-s2.0-77956265586&partnerID=MN8TOARS. 10.1007/s10930-010-9265-1 Domingues, S.; Matos, R.G.; Reis, F.P.; Fialho, A.M.; Barbas, A.; Arraiano, C.M.. "Biochemical characterization of the RNase II family of exoribonucleases from the human pathogens Salmonella typhimurium and Streptococcus pneumoniae". Biochemistry 48 50 (2009): 11848-11857. http://www.scopus.com/inward/record.url?eid=2-s2.0-72449207486&partnerID=MN8TOARS. 10.1021/bi901105n Matos, R.G.; Barbas, A.; Arraiano, C.M.. "RNase R mutants elucidate the catalysis of structured RNA: RNA-binding domains select the RNAs targeted for degradation". Biochemical Journal 423 2 (2009): 291-301. http://www.scopus.com/inward/record.url?eid=2-s2.0-70350111321&partnerID=MN8TOARS. 10.1042/BJ20090839 Barbas, A.; Matos, R.G.; Amblar, M.; López-Viñas, E.; Gomez-Puertas, P.; Arraiano, C.M.. "Determination of key residues for catalysis and RNA cleavage specificity. One mutation turns RNase II Into a "super-enzyme"". Journal of Biological Chemistry 284 31 (2009): 20486-20498. http://www.scopus.com/inward/record.url?eid=2-s2.0-68949127239&partnerID=MN8TOARS. 10.1074/jbc.M109.020693 Schaeffer, D.; Tsanova, B.; Barbas, A.; Reis, F.P.; Dastidar, E.G.; Sanchez-Rotunno, M.; Arraiano, C.M.; Van Hoof, A.. "The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities". Nature Structural and Molecular Biology 16 1 (2009): 56-62. http://www.scopus.com/inward/record.url?eid=2-s2.0-58149236691&partnerID=MN8TOARS. 10.1038/nsmb.1528 Barbas, A.; Matos, R.G.; Amblar, M.; López-Viñas, E.; Gomez-Puertas, P.; Arraiano, C.M.. "New insights into the mechanism of RNA degradation by ribonuclease II: Identification of the residue responsible for setting the RNase II end product". Journal of Biological Chemistry 283 19 (2008): 13070-13076. http://www.scopus.com/inward/record.url?eid=2-s2.0-45149086359&partnerID=MN8TOARS. 10.1074/jbc.M709989200 Amblar, M.; Barbas, A.; Gomez-Puertas, P.; Arraiano, C.M.. "The role of the S1 domain in exoribonucleolytic activity: Substrate specificity and multimerization". RNA 13 3 (2007): 317-327. http://www.scopus.com/inward/record.url?eid=2-s2.0-33847247982&partnerID=MN8TOARS. 10.1261/rna.220407 Frazão, C.; McVey, C.E.; Amblar, M.; Barbas, A.; Vonrhein, C.; Arraiano, C.M.; Carrondo, M.A.. "Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex". Nature 443 7107 (2006): 110-114. http://www.scopus.com/inward/record.url?eid=2-s2.0-33748414894&partnerID=MN8TOARS. 10.1038/nature05080 Amblar, M.; Barbas, A.; Fialho, A.M.; Arraiano, C.M.. "Characterization of the Functional Domains of Escherichia coli RNase II". Journal of Molecular Biology 360 5 (2006): 921-933. http://www.scopus.com/inward/record.url?eid=2-s2.0-33745951483&partnerID=MN8TOARS. 10.1016/j.jmb.2006.05.043 McVey, C.E.; Amblar, M.; Barbas, A.; Cairrão, F.; Coelho, R.; Romáo, C.; Arraiano, C.M.; Carrondo, M.A.; Frazão, C.. "Expression, purification, crystallization and preliminary diffraction data characterization of Escherichia coli ribonuclease II (RNase II)". Acta Crystallographica Section F: Structural Biology and Crystallization Communications 62 7 (2006): 684-687. http://www.scopus.com/inward/record.url?eid=2-s2.0-33745684855&partnerID=MN8TOARS. 10.1107/S1744309106021506

Livro

Arraiano, C.M.; Barbas, A.; Amblar, M.. Chapter 8 Characterizing Ribonucleases In Vitro. Examples of Synergies between Biochemical and Structural Analysis. 2008. 10.1016/S0076-6879(08)02208-8

Prémio

2011	Terry Fox Grants 2012 Award for Cancer Research Liga Portuguesa Contra o Cancro, Portugal
2011	L’Oreal Portugal Award for Women in Science Fundação para a Ciência e a Tecnologia, Portugal L'Oreal Canada, Canadá Fondation L'Oréal, França