Artur F. Castro-Rodrigues

ORCID: 0000-0002-1630-3810
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About
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Research Areas
  • Neurobiology and Insect Physiology Research
  • Ion channel regulation and function
  • Cellular transport and secretion
  • Microtubule and mitosis dynamics
  • Alzheimer's disease research and treatments
  • Porphyrin Metabolism and Disorders
  • Cell Adhesion Molecules Research
  • Trace Elements in Health
  • Ferrocene Chemistry and Applications
  • Amyloidosis: Diagnosis, Treatment, Outcomes
  • Cellular Mechanics and Interactions
  • Cardiac electrophysiology and arrhythmias
  • Coagulation, Bradykinin, Polyphosphates, and Angioedema
  • Retinal Development and Disorders
  • Helminth infection and control
  • Hemoglobin structure and function
  • Ion Channels and Receptors
  • Enzyme Structure and Function
  • Receptor Mechanisms and Signaling
  • Botanical Research and Chemistry
  • Parasite Biology and Host Interactions
  • Plant-based Medicinal Research
  • Coccidia and coccidiosis research

i3S - Instituto de Investigação e Inovação em Saúde, Universidade do Porto
2018-2022

Universidade do Porto
2011-2018

Instituto de Biologia Molecular e Celular
2015

Universidade Nova de Lisboa
2003

The MAP kinase and motor scaffold JIP3 prevents excess lysosome accumulation in axons of vertebrates invertebrates. How JIP3's interaction with dynein kinesin-1 contributes to organelle clearance is unclear. We show that human light intermediate chain (DLIC) binds the N-terminal RH1 domain JIP3, its paralog JIP4, lysosomal adaptor RILP. A point mutation abrogates DLIC binding without perturbing between kinesin heavy chain. Characterization this separation-of-function Caenorhabditis elegans...

10.1083/jcb.202110057 article EN cc-by-nc-sa The Journal of Cell Biology 2022-07-13

KCNH channels form an important family of voltage gated potassium channels. These include a N-terminal Per-Arnt-Sim (PAS) domain with unknown function. In other proteins PAS domains are implicated in cellular responses to environmental queues through small molecule binding or involvement signaling cascades. To better understand their role we characterized the structural properties several channel domains. We determined high resolution structures from mouse EAG (mEAG), drosophila ELK (dELK)...

10.1371/journal.pone.0059265 article EN cc-by PLoS ONE 2013-03-15

This work reports the detection of specific immunoglobulins (Ig) against rFh8, a recombinant Fasciola hepatica adult worm excretion–secretion antigen, in sera from experimentally (rabbit, Wistar rat, cattle, and sheep), or naturally (human) infected hosts. In case laboratory experimental models study revealed significant differences between rabbits, which recognized antigen all along infection, rats, showed high anti-rFh8 Ig levels only for short period infection. Available cattle sheep, as...

10.1645/ge-136r article EN Journal of Parasitology 2004-08-01

Human transthyretin (TTR) is a homotetrameric protein that responsible for the formation of amyloid in patients with familiar amyloidotic polyneuropathy (FAP), cardiomyopathy (FAC) and senile systemic amyloidosis (SSA). Amyloid fibrils are characterized by cross-β structure. However, details how TTR monomers organized to form such an assembly remain unknown. The effect Zn(2+) increasing L55P amyloidogenecity has been reported. Crystals L55P-Zn(2+) complex were grown under conditions similar...

10.1107/s090744491104491x article EN Acta Crystallographica Section D Biological Crystallography 2011-11-04

SUMMARY The conserved MAP kinase and motor scaffold JIP3 prevents excess lysosome accumulation in axons of vertebrates invertebrates. Whether how JIP3’s interaction with dynein kinesin-1 contributes to this critical organelle clearance function is unclear. Using purified recombinant human proteins, we show that light intermediate chain (DLIC) binds the N-terminal RH1 domain JIP3, its paralog JIP4, lysosomal adaptor RILP. A point mutation a hydrophobic pocket domain, previously shown abrogate...

10.1101/2021.10.11.463801 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2021-10-11

Cytochrome c" from the obligate methylotroph Methylophilus methylotrophus is a 15 kDa monohaem protein which has c-type haem covalently linked to chain. Two histidine residues are axial ligands of Fe atom in oxidized form. This cytochrome one few known proteins undergoes change spin state upon reduction, with detachment an ligand. Initial crystallization conditions involved utilization cadmium chloride as additive and resulted highly mosaic crystals poor diffraction properties. Optimization...

10.1107/s0907444903001045 article EN Acta Crystallographica Section D Biological Crystallography 2003-02-20
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