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Alain Michel

Researcher at University of Mons

Publications -  26
Citations -  744

Alain Michel is an academic researcher from University of Mons. The author has contributed to research in topics: Peptide sequence & Atrial natriuretic peptide. The author has an hindex of 15, co-authored 26 publications receiving 722 citations. Previous affiliations of Alain Michel include University of Mons-Hainaut.

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Characterization of the ligand-binding site of the transferrin receptor in Trypanosoma brucei demonstrates a structural relationship with the N-terminal domain of the variant surface glycoprotein.

TL;DR: Data provided evidence that the T.brucei Tf receptor is structurally related to the N‐terminal domain of the VSG and that the ligand‐binding site corresponds to the exposed surface loops of the protein.
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Expression analysis of two gene subfamilies encoding the plasma membrane H+‐ATPase in Nicotiana plumbaginifolia reveals the major transport functions of this enzyme

TL;DR: In this paper, the pma-gusA genes were all expressed in root, stem, leaf and flower organs, but each in a cell-type specific manner, and their expression in these organs was confirmed at the protein level using subfamily-specific antibodies.
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Hydrolysis of α-human atrial natriuretic peptide in vitro by human kidney membranes and purified endopeptidase-24.11: evidence for a novel cleavage site

TL;DR: Determination of all the bonds cleaved in alpha-hANP by endopeptidase-24.11 should prove useful for the design of more stable analogues, which could have therapeutic uses in hypertension.
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Characterization of a novel, stage-specific, invariant surface protein in Trypanosoma brucei containing an internal, serine-rich, repetitive motif.

TL;DR: Although present in the flagellar pocket, ISG100 was predominantly associated with components of the pathways for endo/exocytosis, such as intracellular vesicles located in the proximity of the pocket as well a large, electron-lucent perinuclear digestive vacuole.
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Amino acid conservation in animal glucokinases : identification of residues implicated in the interaction with the regulatory protein

TL;DR: In this article, the Xenopus laevis enzyme was cloned and the C-terminal half of the liver glucokinase was identified as a conserved region of the enzyme, which was found to be mainly in the small domain and the hinge region of glueokinase.