The Cleavable N-terminal Domain of Plant Endopolygalacturonases from Clade B May Be Involved in a Regulated Secretion Mechanism
Open Access
- 1 September 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (38) , 35297-35304
- https://doi.org/10.1074/jbc.m102136200
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- The role of pro regions in protein foldingPublished by Elsevier ,2004
- Polygalacturonase and Polygalacturonase Inhibitor Protein: Gene Isolation and Transcription in Glycine max - Heterodera glycines InteractionsMolecular Plant-Microbe Interactions®, 1999
- Cis-elements of protein transport to the plant vacuolesJournal of Experimental Botany, 1999
- Polygalacturonase Gene Expression in Ripe Melon Fruit Supports a Role for Polygalacturonase in Ripening-Associated Pectin DisassemblyPlant Physiology, 1998
- The role of auxin in cell separation in the dehiscence zone of oilseed rape podsJournal of Experimental Botany, 1997
- Characterization of an mRNA encoding a polygalacturonase expressed during pod development in oilseed rape (Brassica napusL.)Journal of Experimental Botany, 1996
- The pro region required for folding of carboxypeptidase Y is a partially folded domain with little regular structural coreBiochemistry, 1993
- The pro region of BPTI facilitates foldingCell, 1992
- Short peptide domains target proteins to plant vacuolesCell, 1992
- In Vitro Synthesis and Processing of Tomato Fruit PolygalacturonasePlant Physiology, 1988