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phytepsin

Known as: HvAP, barley-grain aspartic proteinase 
National Institutes of Health

Related topics

Related topics

2 relations

Broader (2)

Aspartic Acid EndopeptidasesCathepsins

Papers overview

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2013
2013
A novel aspartic acid protease gene from pineapple fruit (Ananas comosus): cloning, characterization and relation to postharvest chilling stress resistance.
2009
2009
Determination of octanol-air partition coefficients and supercooled liquid vapor pressures of organochlorine pesticides
Octanol-air partition coefficients (KOA) and supercooled liquid vapor pressures (PL) of nine organochlorine pesticides (OCPs… 
2003
2003
Characterization of an aspartic proteinase activity in buckwheat (Fagopyrum esculentum Moench) seeds.
The pepstatin A sensitive acidic proteolytic activity of total protein extracts of buckwheat seeds has been analyzed in… 
Highly Cited
2001
Highly Cited
2001
A Vacuolar Sorting Domain May Also Influence the Way in Which Proteins Leave the Endoplasmic Reticulum
Protein sorting to plant vacuoles is known to be dependent on a considerable variety of protein motifs recognized by a family of… 
Highly Cited
1999
Highly Cited
1999
Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting
We determined at 2.3 Å resolution the crystal structure of prophytepsin, a zymogen of a barley vacuolar aspartic proteinase. In… 
Highly Cited
1998
Highly Cited
1998
Phytepsin, a barley vacuolar aspartic proteinase, is highly expressed during autolysis of developing tracheary elements and sieve cells.
Vacuolarisation, formation of autophagocytotic vacuoles and tonoplast disruption have been reported in plant cells undergoing… 
Highly Cited
1998
Highly Cited
1998
Transport and Activation of the Vacuolar Aspartic Proteinase Phytepsin in Barley (Hordeum vulgare L.)*
The primary translation product of barley aspartic proteinase, phytepsin (EC 3.4.23.40), consists of a signal sequence, a propart… 
Highly Cited
1995
Highly Cited
1995
Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal and microbial aspartic proteinases.
The gene organization and nucleotide sequence of an aspartic proteinase (AP) of plant origin were first disclosed by cDNA and… 
Highly Cited
1994
Highly Cited
1994
The Aspartic Proteinase of Barley Is a Vacuolar Enzyme That Processes Probarley Lectin in Vitro
Previous work suggested that the aspartic proteinase from Hordeum vulgare (HvAP) would be a vacuolar protein in plant cells… 
Highly Cited
1993
Highly Cited
1993
Hydrolytic specificity of the barley grain aspartic proteinase.
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