ArticlePlant molecular biology2000
Identification of a novel four-domain member of the proteinase inhibitor II family from the stigmas of Nicotiana alata.
Article in Plant molecular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed.
- Novel in vitro inhibitory functions of potato tuber proteinaceous inhibitors.Molecular genetics and genomics : MGG · 2015Article
- Article
- Stress inducible proteinase inhibitor diversity in Capsicum annuum.BMC plant biology · 2012Article
- Coexpression of potato type I and II proteinase inhibitors gives cotton plants protection against insect damage in the field.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Tandem duplication, circular permutation, molecular adaptation: how Solanaceae resist pests via inhibitors.BMC bioinformatics · 2008Article
- Pollination in Nicotiana alata stimulates synthesis and transfer to the stigmatic surface of NaStEP, a vacuolar Kunitz proteinase inhibitor homologue.Journal of experimental botany · 2008Article
- Dual location of a family of proteinase inhibitors within the stigmas of Nicotiana alata.Planta · 2007Article
- Evolution of proteinase inhibitor defenses in North American allopolyploid species of Nicotiana.Planta · 2006Article
- Differential elicitation of two processing proteases controls the processing pattern of the trypsin proteinase inhibitor precursor in Nicotiana attenuata.Plant physiology · 2005Article
- Manipulation of endogenous trypsin proteinase inhibitor production in Nicotiana attenuata demonstrates their function as antiherbivore defenses.Plant physiology · 2004Article
- Pistil factors controlling pollination.The Plant cell · 2004Review
- Three classes of proteinase inhibitor gene have distinct but overlapping patterns of expression in Pisum sativum plants.Plant molecular biology · 2002Article
- A proteinase inhibitor II of Solanum americanum is expressed in phloem.Plant molecular biology · 2001Article
- Proteins of circularly permuted sequence present within the same organism: the major serine proteinase inhibitor from Capsicum annuum seeds.Protein science : a publication of the Protein Society · 2001Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteinase inhibitors (PIs) of the potato type II family have been identified in a number of solanaceous species. Most family members have two PI domains which are specific for either chymotrypsin or trypsin. More recently family members have been described with three or six repeated PI domains. Here we describe a novel four-domain family member produced in the stigmas and leaves of the ornamental tobacco, Nicotiana alata, which has high sequence identity with a six-domain member from the same species. Both proteins are produced as precursors that enter the secretory pathway and are subsequently processed into a series of 6 kDa Pis. The four- and six-domain precursor proteins were isolated from immature stigmas and characterised by mass spectrometry which revealed that both proteins had been trimmed at the N-terminus, at a position corresponding to the predicted signal peptide cleavage site. Furthermore, no post-translational modifications were apparent.
Indexed as
Identifiers
10794532What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.