A. J. Parodi

发表

The molecular basis for the recognition of misfolded glycoproteins by the UDP‐Glc:glycoprotein glucosyltransferase.

M. Sousa, A. J. Parodi, A. Parodi, 1995, The EMBO journal.

N-glycosylation in trypanosomatid protozoa.

A. J. Parodi, A. Parodi, 1993, Glycobiology.

The quality control of glycoprotein folding in the endoplasmic reticulum, a trip from trypanosomes to mammals.

A. J. Parodi, 1998, Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas.

The presence of complex-type oligosaccharides at the C-terminal domain glycosylation site of some molecules of cruzipain.

A. J. Parodi, J. Cazzulo, C. Labriola, 1995, Molecular and biochemical parasitology.

Reglucosylation of glycoproteins and quality control of glycoprotein folding in the endoplasmic reticulum of yeast cells.

A. J. Parodi, A. Parodi, 1999, Biochimica et biophysica acta.

Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation.

A. J. Parodi, A. Parodi, 2000, The Biochemical journal.

Protein glucosylation and its role in protein folding.

A. J. Parodi, A. Parodi, 2000, Annual review of biochemistry.

A new stress protein: synthesis of Schizosaccharomyces pombe UDP–Glc:glycoprotein glucosyltransferase mRNA is induced by stress conditions but the enzyme is not essential for cell viability.

U. Hellman, A. J. Parodi, A. Parodi, 1996, The EMBO journal.

Identification of the gene(s) coding for the trans‐sialidase of Trypanosoma cruzi.

D. Sánchez, G. Pollevick, A. C. Frasch, 1992, The EMBO journal.