Rosangela A S Eichler
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Explore the profile of Rosangela A S Eichler including associated specialties, affiliations and a list of published articles.
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8
Citations
44
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Recent Articles
1.
Eichler R, Martucci L, de Castro L, Ferro E
Methods Mol Biol
. 2024 Mar;
2758:199-212.
PMID: 38549015
Peptides have broad biological significance among different species. Intracellular peptides are considered a particular class of bioactive peptides, whose generation is initiated by proteasomal degradation of cytosolic, nuclear, or mitochondrial...
2.
Caprioli B, Eichler R, Silva R, Martucci L, Reckziegel P, Ferro E
Int J Mol Sci
. 2023 Oct;
24(20).
PMID: 37894869
Neurolysin oligopeptidase (E.C.3.4.24.16; Nln), a member of the zinc metallopeptidase M3 family, was first identified in rat brain synaptic membranes hydrolyzing neurotensin at the Pro-Tyr peptide bond. The previous development...
3.
Martucci L, Eichler R, Silva R, Costa T, Tostes R, Busatto G, et al.
iScience
. 2023 Aug;
26(9):107542.
PMID: 37636076
Intracellular peptides (InPeps) generated by the orchestrated action of the proteasome and intracellular peptidases have biological and pharmacological significance. Here, human plasma relative concentration of specific InPeps was compared between...
4.
Parada C, de Oliveira I, Gewehr M, Machado-Neto J, Lima K, Eichler R, et al.
Cells
. 2022 Feb;
11(3).
PMID: 35159195
Intracellular peptides (InPeps) generated by proteasomes were previously suggested as putative natural regulators of protein-protein interactions (PPI). Here, the main aim was to investigate the intracellular effects of intracellular peptide...
5.
Silva R, Llanos R, Eichler R, Oliveira T, Gozzo F, Festuccia W, et al.
Pharmaceutics
. 2021 Dec;
13(12).
PMID: 34959456
Intracellular peptides were shown to derive from proteasomal degradation of proteins from mammalian and yeast cells, being suggested to play distinctive roles both inside and outside these cells. Here, the...
6.
Gewehr M, Teixeira A, Santos B, Biondo L, Gozzo F, Cordibello A, et al.
Biomolecules
. 2020 Feb;
10(2).
PMID: 32079362
Thimet oligopeptidase (EC 3.4.24.15; EP24.15; THOP1) is a potential therapeutic target, as it plays key biological functions in processing biologically functional peptides. The structural conformation of THOP1 provides a unique...
7.
Dos Santos N, Franco R, Camarini R, Munhoz C, Eichler R, Gewehr M, et al.
Biomolecules
. 2019 Aug;
9(8).
PMID: 31431000
Thimet oligopeptidase (THOP1) is thought to be involved in neuropeptide metabolism, antigen presentation, neurodegeneration, and cancer. Herein, the generation of THOP1 C57BL/6 knockout mice (THOP1) is described showing that they...
8.
Reckziegel P, Festuccia W, Britto L, Jang K, Romao C, Heimann J, et al.
Sci Rep
. 2017 Nov;
7(1):14781.
PMID: 29093454
Intracellular peptides generated by limited proteolysis are likely to function inside and outside cells and could represent new possibilities for drug development. Here, we used several conformational-sensitive antibodies targeting G-protein...