Cecília R. Santos

Dr. Cecília R. Santos

CICS-UBI- Health Sciences Research Centre, University of Beira Interior
orcid

Research Focus & Metrics

Academic Career Length

32Years (1995-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 September 2000 in General and Comparative Endocrinology
Verified
Journal Article
Closed access
DPDeborah Mary Power
Deborah Mary Power
NEN.P. Elias
N.P. Elias
Samantha RichardsonSamantha Richardson
Samantha Richardson
JMJ. Mendes
J. Mendes
CSClaudio Soares
Claudio Soares
Cecília R. SantosCecília R. Santos
Cecília R. Santos

1 May 2012 in Molecular Cancer Research
Verified
Journal Article
Closed access
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IGInês M. Gomes
Inês M. Gomes
Cláudio MaiaCláudio Maia
Cláudio Maia
Cecília R. SantosCecília R. Santos
Cecília R. Santos
The human 6-transmembrane epithelial antigen of prostate (STEAP) family comprises STEAP1, STEAP2, STEAP3, and STEAP4. All of these proteins are unique to mammals and share an innate activity as metalloreductases, indicating their importance in metal metabolism. Overall, they participate in a wide range of biologic processes, such as molecular trafficking in the endocytic and exocytic pathways and control of cell proliferation and apoptosis. STEAP1 and STEAP2 are overexpressed in several types of human cancers, namely prostate, bladder, colon, pancreas, ovary, testis, breast, cervix, and Ewing sarcoma, but their clinical significance and role in cancer cells are not clear. Still, their localization in the cell membrane and differential expression in normal and cancer tissues make STEAP proteins potential candidates as biomarkers of several cancers, as well as potential targets for new immunotherapeutic strategies for disease attenuation or treatment. This review brings together the current knowledge about each STEAP protein, giving an overview of the roles of this family of proteins in human physiology and disease, and analyzes their potential as immunotherapeutic agents in cancer research. Mol Cancer Res; 10(5); 573–87. ©2012 AACR.

1 November 2017 in Neurobiology of Disease
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Journal Article
Closed access
FMFernanda Marques
Fernanda Marques
JSJoão Carlos Sousa
João Carlos Sousa
MBMaria Brito
Maria Brito
Jens PahnkeJens Pahnke
Jens Pahnke
Cecília R. SantosCecília R. Santos
Cecília R. Santos
JPJoana Almeida Palha
Joana Almeida Palha

1 June 2007 in General and Comparative Endocrinology
Verified
Journal Article
Closed access
IMI. Morgado
I. Morgado
Cecília R. SantosCecília R. Santos
Cecília R. Santos
RJR. Jacinto
R. Jacinto
DPDeborah Mary Power
Deborah Mary Power

1 June 2004 in Journal of Biological Chemistry
Verified
Journal Article
Open access
PDF file
TETherese Eneqvist
Therese Eneqvist
ELErik Lundberg
Erik Lundberg
AKAnders Karlsson
Anders Karlsson
SHShenghua Huang
Shenghua Huang
Cecília R. SantosCecília R. Santos
Cecília R. Santos
ASA. Elisabeth Sauer-Eriksson
A. Elisabeth Sauer-Eriksson
Transthyretin (TTR) is an extracellular transport protein involved in the distribution of thyroid hormones and vitamin A. So far, TTR has only been found in vertebrates, of which piscine TTR displays the lowest sequence identity with human TTR (47%). Human and piscine TTR bind both thyroid hormones 3,5,3′-triiodo-l-thyronine (T3) and 3,5,3′,5′-tetraiodo-l-thyronine (thyroxine, T4). Human TTR has higher affinity for T4 than T3, whereas the reverse holds for piscine TTR. X-ray structures of Sparus aurata (sea bream) TTR have been determined as the apo-protein at 1.75 Å resolution and bound to ligands T3 and T4, both at 1.9 Å resolution. The apo structure is similar to human TTR with structural changes only at β-strand D. This strand forms an extended loop conformation similar to the one in chicken TTR. The piscine TTR·T4 complex shows the T4-binding site to be similar but not identical to human TTR, whereas the TTR·T3 complex shows the I3′ halogen situated at the site normally occupied by the hydroxyl group of T4. The significantly wider entrance of the hormone-binding channel in sea bream TTR, in combination with its narrower cavity, provides a structural explanation for the different binding affinities of human and piscine TTR to T3 and T4.

1 October 2020 in Trends in Endocrinology & Metabolism
Verified
Journal Article
Closed access
ACAna R. Costa
Ana R. Costa
MOMariana Lança de Oliveira
Mariana Lança de Oliveira
ICInês Cruz
Inês Cruz
IGIsabel Goncalves
Isabel Goncalves
JCJosé Cascalheira
José Cascalheira
Cecília R. SantosCecília R. Santos
Cecília R. Santos