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Armando J. Parodi

Researcher at Fundación Instituto Leloir

Publications -  43
Citations -  2420

Armando J. Parodi is an academic researcher from Fundación Instituto Leloir. The author has contributed to research in topics: Endoplasmic reticulum & UGGT. The author has an hindex of 25, co-authored 43 publications receiving 2299 citations. Previous affiliations of Armando J. Parodi include National Scientific and Technical Research Council.

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Journal ArticleDOI

Getting in and out from calnexin/calreticulin cycles.

TL;DR: Lectin-glycoprotein association not only thwarts Golgi exit of folding intermediates and irreparably misfolded glycoproteins but also enhances folding efficiency by preventing aggregation and promoting proper disulfide bonding.
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The Activity of a Putative Polyisoprenol-linked Sugar Translocase (Wzx) Involved in Escherichia coli O Antigen Assembly Is Independent of the Chemical Structure of the O Repeat

TL;DR: It is demonstrated that a single sugar, GlcNAc, can be incorporated to LPS of Escherichia coli K-12 and suggested that a model for O antigen synthesis involving recognition of Und-P-p-linked sugars by a putative complex made of Wzx translocase and other proteins involved in the processing of O antigen is suggested.
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UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates.

TL;DR: It was confirmed that BiP (binding protein, a chaperone of the heat shock protein 70 family) preferentially recognized neoglycoproteins displaying extended conformations, thus providing a molecular rationale for the sequential BiP-CNX/CRT interaction with folding glycoprotein observed in vivo.
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Structural Characterization of the Major Glycosylphosphatidylinositol Membrane-anchored Glycoprotein from Epimastigote Forms of Trypanosoma cruzi Y-strain

TL;DR: The kinetics of in vitro sialylation of these O-linked oligosaccharides by the T. cruzi trans-sialidase are investigated and it is shown that incorporation of one molecule of sialic acid hinders entry of a second molecule when two potential acceptor sites are present.
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UDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control

TL;DR: The N-glycan-dependent quality control of glycoprotein folding prevents endoplasmic to Golgi exit of folding intermediates, irreparably misfolded glycoproteins and incompletely assembled multimeric complexes and enhances folding efficiency by preventing aggregation and facilitating formation of proper disulfide bonds.