Paulo C. Almeida

ORCID: 0000-0002-3107-3312
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • Protease and Inhibitor Mechanisms
  • Peptidase Inhibition and Analysis
  • Neuropeptides and Animal Physiology
  • Protein Hydrolysis and Bioactive Peptides
  • Coagulation, Bradykinin, Polyphosphates, and Angioedema
  • Cell Adhesion Molecules Research
  • Calpain Protease Function and Regulation
  • Enzyme Production and Characterization
  • Iron Metabolism and Disorders
  • Protein Interaction Studies and Fluorescence Analysis
  • Trypanosoma species research and implications
  • Blood Coagulation and Thrombosis Mechanisms
  • Metal complexes synthesis and properties
  • Renin-Angiotensin System Studies
  • Academic Research in Diverse Fields
  • Cellular transport and secretion
  • Selenium in Biological Systems
  • Adenosine and Purinergic Signaling
  • Molecular Junctions and Nanostructures
  • Organometallic Compounds Synthesis and Characterization
  • Tailings Management and Properties
  • Phytase and its Applications
  • Pancreatic function and diabetes
  • Fire effects on ecosystems
  • Enzyme function and inhibition

University of Aveiro
2024

Weatherford College
2018

University of Regina
2018

Kimberly-Clark (Canada)
2018

Universidade Federal de São Paulo
2011-2013

Universidade de Mogi das Cruzes
1999-2011

Universidade Federal do Paraná
2010

Eletrobras (Brazil)
2002

Ann Arbor Center for Independent Living
2002

University of Michigan
2002

It has been shown that lysosomal cysteine proteinases, specially cathepsin B, implicated in a variety of diseases involving tissue remodeling states, such as inflammation, parasite infection, and tumor metastasis, by degradation extracellular matrix components. Recently, we have heparin heparan sulfate bind to papain specifically; this interaction induces an increase its alpha-helix content stabilizes the enzyme structure even at alkaline pH (Almeida, P. C., Nantes, I. L., Rizzi, C. A.,...

10.1074/jbc.m003820200 article EN cc-by Journal of Biological Chemistry 2001-01-01

Endopeptidase 24.15 (EC; ep24.15), neurolysin ep24.16), and angiotensin-converting enzyme ACE) are metallopeptidases involved in neuropeptide metabolism vertebrates. Using catalytically inactive forms of ep24.15 ep24.16, we have identified new peptide substrates for these enzymes. The enzymatic activity ep24.16 was inactivated by site-directed mutagenesis amino acid residues within their conserved HEXXH motifs, without disturbing secondary structure or binding ability, as shown circular...

10.1074/jbc.m212030200 article EN cc-by Journal of Biological Chemistry 2003-02-28

<i>Trypanosoma cruzi</i> activates the kinin pathway through activity of its major cysteine proteinase, cruzipain. Because kininogen molecules may be displayed on cell surfaces by binding to glycosaminoglycans, we examined whether ability cruzipain release kinins from high molecular weight (HK) is modulated heparan sulfate (HS). Kinetic assays show that HS reduces proteinase inhibitory (<i>K</i> <sub>i</sub> <sub>app</sub>) HK about 10-fold. Conversely, catalytic efficiency kinin-related...

10.1074/jbc.m108518200 article EN cc-by Journal of Biological Chemistry 2002-02-01

Kinetic data for the hydrolysis by human tissue kallikrein of fluorogenic peptides with o-aminobenzoyl-Phe-Arg (Abz-FR) as acyl group and different leaving groups demonstrate that interactions S'1, S'2 S'3 subsites are important cleavage efficiency. In addition, studies on kininogen sequence spanning scissile Met-Lys bond [Abz-M-I-S-L-M-K-R-P-N-(2,4-dinitrophenyl)ethylenediamine] analogues residues at positions P'1, P'2 P'3 showed (a) presence a proline residue kallikrein-binding sites S2 to...

10.1042/bj3060063 article EN Biochemical Journal 1995-02-15

Papain is considered to be the archetype of cysteine proteinases. The interaction heparin and other glycosaminoglycans with papain may representative many mammalian proteinase-glycosaminoglycan interactions that can regulate function this class proteinases in vivo. conformational changes structure due glycosaminoglycan were studied by circular dichroism spectroscopy, enzyme behavior kinetic analysis, monitored fluorogenic substrate. presence significantly increases α-helix content papain....

10.1074/jbc.274.43.30433 article EN cc-by Journal of Biological Chemistry 1999-10-01

Background Cysteine protease B is considered crucial for the survival and infectivity of Leishmania in its human host. Several microorganism pathogens bind to heparin-like glycosaminoglycans chains proteoglycans at host-cell surface promote their attachment internalization. Here, we have investigated influence heparin upon mexicana cysteine rCPB2.8 activity. Methodology/Principal Findings The data analysis revealed that presence affects all steps enzyme reaction: (i) it decreases 3.5-fold k1...

10.1371/journal.pone.0080153 article EN cc-by PLoS ONE 2013-11-21

Heparin has been shown to regulate human neutrophil elastase (HNE) activity. We have assessed the regulatory effect of heparin on Tissue Inhibitor Metalloproteases-1 [TIMP-1] hydrolysis by HNE employing recombinant form TIMP-1 and correlated FRET-peptides comprising cleavage site. accelerates 2.5-fold HNE. The kinetic parameters this reaction were monitored with aid a FRET-peptide substrate that mimics site in pre-steady-state conditionsby using stopped-flow fluorescence system. exhibits...

10.1371/journal.pone.0021525 article EN cc-by PLoS ONE 2011-06-23

Wildfire ignitions are often linked to environmental and climatic factors, but human behavior plays a critical role, particularly in rural southern Europe. However, tools quantify the probability of human-caused lacking. This study addresses this by developing wildfire ignition index focused on mainland Portugal, region historically vulnerable wildfires. Statistical analyses, including multicollinearity checks Generalized Linear Model, were used analyze data, while geospatial analyses...

10.3390/fire7120447 article EN cc-by Fire 2024-11-29

The metalloendopeptidase 24.15 (EP24.15) is ubiquitously present in the extracellular environment as a secreted protein. Outside cell, this enzyme degrades several neuropeptides containing from 5 to 17 amino acids (e.g. gonadotropin releasing hormone, bradykinin, opioids and neurotensin). constitutive secretion of EP24.15 glioma C6 cells was demonstrated be stimulated linearly by reduced concentrations calcium. In report we demonstrate that calcium concentration has no effect on total amount...

10.1111/j.1742-4658.2005.04692.x article EN FEBS Journal 2005-06-01

Cathepsin B is a lysosomal thiolprotease that, because of its colocalization with renin and ability to activate prorenin, has been proposed as prorenin processing enzyme. To characterize the biochemical aspect this potential cathepsin activity in more detail, we synthesized assayed human internally quenched fluorescent peptide Abz-FSQPMKRLTLGNTTQ-EDDnp (Abz, ortho-aminobenzoic acid group EDDnp, N-¿2, 4-dinitrophenyl-ethylenediamine quencher group) that contains 7 amino acids for each side...

10.1161/01.hyp.35.6.1278 article EN Hypertension 2000-06-01

We combined fluorogenic substrates or internally quenched fluorescent peptides with specific inhibitors in the pH profile of proteolytic activity experiments order to detect activities lysates MDCK cells. Hydrolytic related cathepsin B, L, and D were observed. Serine-proteinase was not detected; however, we clearly demonstrated presence a thiol-metallo-endo-oligopeptidase, also called thimet-oligopeptidase (TOP). This peptidase from cells has substrate inhibitor specificities as well an...

10.1002/(sici)1097-4644(20000301)76:3<478::aid-jcb14>3.0.co;2-h article EN Journal of Cellular Biochemistry 2000-03-01

We combined fluorogenic substrates or internally quenched fluorescent peptides with specific inhibitors in the pH profile of proteolytic activity experiments order to detect activities lysates MDCK cells. Hydrolytic related cathepsin B, L, and D were observed. Serine-proteinase was not detected; however, we clearly demonstrated presence a thiol-metallo-endo-oligopeptidase, also called thimet-oligopeptidase (TOP). This peptidase from cells has substrate inhibitor specificities as well an...

10.1002/(sici)1097-4644(20000301)76:3<478::aid-jcb14>3.3.co;2-8 article EN Journal of Cellular Biochemistry 2000-03-01

This paper reports on the development of 440 kV Bauru substation security control scheme, Brazil, as well all changes in physical layout and protection systems that are to be made before installation this scheme.

10.1109/ptc.2001.964771 article EN 2002-11-13
Coming Soon ...