ArticleGenetics1999
Mutational analysis of the [Het-s] prion analog of Podospora anserina. A short N-terminal peptide allows prion propagation.
Article in Genetics, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed.
- Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective.Frontiers in molecular neuroscience · 2021Review
- All-atom simulation of the HET-s prion replication.PLoS computational biology · 2020Article
- Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.PLoS pathogens · 2014Article
- The mechanism of toxicity in HET-S/HET-s prion incompatibility.PLoS biology · 2012Article
- Localization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity.Molecular and cellular biology · 2012Article
- A method for probing the mutational landscape of amyloid structure.Bioinformatics (Oxford, England) · 2011Article
- Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- The mechanism of prion inhibition by HET-S.Molecular cell · 2010Article
- WD-repeat instability and diversification of the Podospora anserina hnwd non-self recognition gene family.BMC evolutionary biology · 2010Article
- Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast.Molecular biology of the cell · 2010Article
- Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+].Nature structural & molecular biology · 2009Article
- A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast.Molecular cell · 2007Article
- Het up mould unleashes a sporekiller prion.Journal of biosciences · 2003Article
- Sexual transmission of the [Het-S] prion leads to meiotic drive in Podospora anserina.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Nonself recognition is mediated by HET-C heterocomplex formation during vegetative incompatibility.The EMBO journal · 2002Article
- Identification of vib-1, a locus involved in vegetative incompatibility mediated by het-c in Neurospora crassa.Genetics · 2002Article
- Progress toward an ultimate proof of the prion hypothesis.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Molecular genetics of heterokaryon incompatibility in filamentous ascomycetes.Microbiology and molecular biology reviews : MMBR · 2000Review
- Review
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
The het-s locus is one of nine known het (heterokaryon incompatibility) loci of the fungus Podospora anserina. This locus exists as two wild-type alleles, het-s and het-S, which encode 289 amino acid proteins differing at 13 amino acid positions. The het-s and het-S alleles are incompatible as their coexpression in the same cytoplasm causes a characteristic cell death reaction. We have proposed that the HET-s protein is a prion analog. Strains of the het-s genotype exist in two phenotypic states, the neutral [Het-s*] and the active [Het-s] phenotype. The [Het-s] phenotype is infectious and is transmitted to [Het-s*] strains through cytoplasmic contact. het-s and het-S were associated in a single haploid nucleus to generate a self-incompatible strain that displays a restricted and abnormal growth. In the present article we report the molecular characterization of a collection of mutants that restore the ability of this self-incompatible strain to grow. We also describe the functional analysis of a series of deletion constructs and site-directed mutants. Together, these analyses define positions critical for reactivity and allele specificity. We show that a 112-amino-acid-long N-terminal peptide of HET-s retains [Het-s] activity. Moreover, expression of a mutant het-s allele truncated at position 26 is sufficient to allow propagation of the [Het-s] prion analog.
Indexed as
Identifiers
What 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.