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Abbreviation : SPP
Long Form : stromal processing peptidase
No. Year Title Co-occurring Abbreviation
2018 Chloroplast stromal processing peptidase activity is modulated by transit peptide determinants that include inhibitory roles for its N-terminal domain and initial Met. ---
2011 The stromal processing peptidase of chloroplasts is essential in Arabidopsis, with knockout mutations causing embryo arrest after the 16-cell stage. ---
2010 A rice stromal processing peptidase regulates chloroplast and root development. LHCP
2007 A novel serine/proline-rich domain in combination with a transmembrane domain is required for the insertion of AtTic40 into the inner envelope membrane of chloroplasts. ---
2005 Protein import pathways in 'complex' chloroplasts derived from secondary endosymbiosis involving a red algal ancestor. ---
2004 Processing of the dual targeted precursor protein of glutathione reductase in mitochondria and chloroplasts. GR, MPP
2003 A pea antisense gene for the chloroplast stromal processing peptidase yields seedling lethals in Arabidopsis: survivors show defective GFP import in vivo. GFP
2003 Structural properties of the chloroplast stromal processing peptidase required for its function in transit peptide removal. ---
2002 Determinants for removal and degradation of transit peptides of chloroplast precursor proteins. ---
10  2002 Processing of an apicoplast leader sequence in Plasmodium falciparum and the identification of a putative leader cleavage enzyme. ---
11  2000 Chloroplasts of the green alga Chlamydomonas reinhardtii possess at least four distinct stromal processing proteases. ---
12  1999 Stromal processing peptidase binds transit peptides and initiates their ATP-dependent turnover in chloroplasts. ---
13  1998 Purification and properties of a novel chloroplast stromal peptidase. Processing of polyphenol oxidase and other imported precursors. PPOs, pPPO
14  1994 Efficient but aberrant cleavage of mitochondrial precursor proteins by the chloroplast stromal processing peptidase. MPP
15  1994 Mutations at the stromal processing peptidase cleavage site of a thylakoid lumen protein precursor affect the rate of processing but not the fidelity. ---