N. Varejão

发表

DNA activates the Nse2/Mms21 SUMO E3 ligase in the Smc5/6 complex

D. Reverter, Neus Colomina, Jordi Torres-Rosell, 2018, The EMBO journal.

Tolcapone, a potent aggregation inhibitor for the treatment of familial leptomeningeal amyloidosis

A. Velázquez‐Campoy, D. Reverter, S. Ventura, 2020, The FEBS journal.

Structural Mechanism for the Temperature-Dependent Activation of the Hyperthermophilic Pf2001 Esterase.

D. Foguel, D. Reverter, R. V. Almeida, 2018, Structure.

pCramoll and rCramoll lectins induce cell death in human prostate adenocarcinoma (PC-3) cells by impairment of mitochondrial homeostasis.

F. Rossato, A. Vercesi, Rute A P Costa, 2017, Toxicology in vitro : an international journal published in association with BIBRA.

Development of a Highly Potent Transthyretin Amyloidogenesis Inhibitor: Design, Synthesis, and Evaluation

A. Velázquez‐Campoy, M. Sodupe, D. Reverter, 2022, Journal of medicinal chemistry.

The Importance of a Gatekeeper Residue on the Aggregation of Transthyretin

Y. Cordeiro, D. Foguel, C. Braga, 2014, The Journal of Biological Chemistry.

Structural basis for the E3 ligase activity enhancement of yeast Nse2 by SUMO-interacting motifs

G. Bellí, D. Reverter, Jordi Torres-Rosell, 2021, Nature Communications.

Molecular mechanisms in SUMO conjugation.

D. Reverter, N. Varejão, Jara Lascorz, 2019, Biochemical Society transactions.

Encapsulation into Stealth Liposomes Enhances the Antitumor Action of Recombinant Cratylia mollis Lectin Expressed in Escherichia coli

M. Correia, L. Coelho, L. C. D. da Silva, 2016, Front. Microbiol..

Characterization of the unfolding process of the tetrameric and dimeric forms of Cratylia mollis seed lectin (CRAMOLL 1): effects of natural fragmentation on protein stability.

D. Foguel, M. Correia, N. Varejão, 2011, Biochemistry.

Heterologous expression and purification of a biologically active legume lectin from Cratylia mollis seeds (CRAMOLL 1).

M. Almeida, D. Foguel, G. Atella, 2010, Biochimica et biophysica acta.

Disease-associated mutations impacting BC-loop flexibility trigger long-range transthyretin tetramer destabilization and aggregation

E. Papaleo, G. Rivas, Valentina Sora, 2021, The Journal of biological chemistry.

Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation

M. de Carvalho, D. Foguel, D. Reverter, 2017, Scientific Reports.

Structure-Based Analysis of A19D, a Variant of Transthyretin Involved in Familial Amyloid Cardiomyopathy

D. Foguel, S. Ventura, F. Rumjanek, 2013, PloS one.

Combining Structural Aggregation Propensity and Stability Predictions To Redesign Protein Solubility.

Salvador Ventura, Sebastian Kmiecik, Marta Díaz-Caballero, 2018, Molecular pharmaceutics.

Structural basis for the SUMO protease activity of the atypical ubiquitin-specific protease USPL1

D. Reverter, N. Varejão, Ying Li, 2022, Nature Communications.

Chemical tools for structural studies of ubiquitin and ubiquitin-like deconjugating proteases

D. Reverter, N. Varejão, Helena Borràs-Gas, 2023, Current Research in Chemical Biology.

Broad-spectrum ubiquitin/ubiquitin-like deconjugation activity of the rhizobial effector NopD from Bradyrhizobium (sp. XS1150)

D. Reverter, N. Varejão, L. M. Lois, 2024, Communications biology.