Weitere Beiträge zum Kapitel „Spastische Pseudosklerose Jakobs”

Stender, A

doi:10.1007/bf02864285

Cited by 24 publications

(6 citation statements)

References 3 publications

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“…By 1930, the high incidence of familial (f) CJD in some families was known (1,2). Almost 60 years were to pass before the significance of this finding could be appreciated (3)(4)(5).…”

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confidence: 99%

“…4B). Familial CJD cases suggested that genetic factors might influence pathogenesis (1,2,244), but this was difficult to reconcile with the transmissibility of fCJD and GSS (3). The discovery of genetic linkage between the PrP gene and scrapie incubation times in mice (213) raised the possibility that mutation might feature in the hereditary human prion diseases.…”

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confidence: 99%

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Prions

Prusiner

1998

Proc. Natl. Acad. Sci. U.S.A.

5,341

4,235

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Prions are unprecedented infectious pathogens that cause a group of invariably fatal neurodegenerative diseases by an entirely novel mechanism. Prion diseases may present as genetic, infectious, or sporadic disorders, all of which involve modification of the prion protein (PrP). Bovine spongiform encephalopathy (BSE), scrapie of sheep, and Creutzfeldt-Jakob disease (CJD) of humans are among the most notable prion diseases. Prions are transmissible particles that are devoid of nucleic acid and seem to be composed exclusively of a modified protein (PrP Sc ). The normal, cellular PrP (PrP C ) is converted into PrP Sc through a posttranslational process during which it acquires a high ␤-sheet content. The species of a particular prion is encoded by the sequence of the chromosomal PrP gene of the mammals in which it last replicated. In contrast to pathogens carrying a nucleic acid genome, prions appear to encipher strain-specific properties in the tertiary structure of PrP Sc . Transgenetic studies argue that PrP Sc acts as a template upon which PrP C is refolded into a nascent PrP Sc molecule through a process facilitated by another protein. Miniprions generated in transgenic mice expressing PrP, in which nearly half of the residues were deleted, exhibit unique biological properties and should facilitate structural studies of PrP Sc . While knowledge about prions has profound implications for studies of the structural plasticity of proteins, investigations of prion diseases suggest that new strategies for the prevention and treatment of these disorders may also find application in the more common degenerative diseases.

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“…By 1930, the high incidence of familial (f) CJD in some families was known (1,2). Almost 60 years were to pass before the significance of this finding could be appreciated (3)(4)(5).…”

mentioning

confidence: 99%

mentioning

confidence: 99%

Prions

Prusiner

1998

Proc. Natl. Acad. Sci. U.S.A.

5,341

4,235

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“…The wide variety of presentations manifested by the human prion diseases as genetic, sporadic, and infectious illnesses is unprecedented. As early as 1930, familial clusters of CJD were recognized (Meggendorfer 1930;Stender 1930), but the subsequent transmission of CJD to apes shifted thinking away from a genetic etiology to that of an atypical virus (Gibbs et al 1968;Masters et al 1981). Subsequently, the identification of mutations in the prion protein (PrP) gene (PRNP) of patients with familial prion disease demonstrated that these diseases are inherited while also transmissible (Hsiao et al 1989;Prusiner 1989).…”

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confidence: 99%

Complete Genomic Sequence and Analysis of the Prion Protein Gene Region from Three Mammalian Species

Lee

Westaway²,

Smit³

et al. 1998

Genome Res.

156

125

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The prion protein (PrP), first identified in scrapie-infected rodents, is encoded by a single exon of a single-copy chromosomal gene. In addition to the protein-coding exon, PrP genes in mammals contain one or two 5′-noncoding exons. To learn more about the genomic organization of regions surrounding the PrP exons, we sequenced 105 bp of DNA from clones containing human, sheep, and mouse PrP genes isolated in cosmids or λ phage. Our findings are as follows: (1) Although the human PrP transcript does not include the untranslated exon 2 found in its mouse and sheep counterparts, the large intron of the human PrP gene contains an exon 2-like sequence flanked by consensus splice acceptor and donor sites. (2) The mouse Prnpa but not thePrnpb allele found in 44 inbred lines contains a 6593 nucleotide retroviral genome inserted into the anticoding strand of intron 2. This intracisternal A-particle element is flanked by duplications of an AAGGCT nucleotide motif. (3) We found that thePrP gene regions contain from 40% to 57% genome-wide repetitive elements that independently increased the size of the locus in all three species by numerous mutations. The unusually long sheepPrP 3′-untranslated region contains a “fossil” 1.2-kb mariner transposable element. (4) We identified sequences in noncoding DNA that are conserved between the three species and may represent biologically functional sites.[The nucleotide sequence data reported in this paper have been submitted to the GenBank sequence database and have been assigned the accession numbers U29185(human), U29186 (mouse), and U67922 (sheep).]

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“…18 In addition, 4 of 5 later cases from Jakob's laboratory [28][29][30][31] also showed the typical pathologic changes of spongiform encephalopathy and demonstrated that his concept of spastic pseudosclerosis evolved to encompass "only cases of typical spongiform encephalopathy." 18 Three of these later confirmed cases were members of a single family [28][29][30][31] ; in 1994, Brown et al 32 at the NIH extracted DNA from preserved tissue in the original pathologic slides and identified a mutation at codon 178 in the PRNP gene of the proband from this family, proving that these were cases of familial human prion disease. By 1923, Jakob believed his cases resembled a "chronic brainstem encephalitis," anticipated the transmissible nature of the disease, and even suggested intracerebral inoculation experiments from his cases to rabbits (i.e., like those done later in the 1960s by Gajdusek, Gibbs, and colleagues using chimpanzees and monkeys, first with kuru and then with CJD).…”

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confidence: 99%

Clarence J. Gibbs Effect and the “Creutzfeldt-Jakob Disease” Eponym

Lanska

2021

Neurology

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In 2014, American neurologist and Nobel laureate Stanley Prusiner reported that microbiologist Clarence Joseph Gibbs at the U.S. National Institutes of Health had intentionally, systematically, and mischievously used the eponym Creutzfeldt-Jakob disease (CJD), rather than Jakob-Creutzfeldt disease (JCD), because of the correspondence with Gibbs’ own initials to imply “Clarence Joseph’s disease.”The present study examines temporal trends in the use of “Creutzfeldt-Jakob” and “Jakob-Creutzfeldt” in scientific articles and monographs from 1946 to 2019 to assess whether there was a “Clarence J. Gibbs’ effect” that influenced the general use of a specific eponym by the scientific community. During Gibbs’ period of publication on CJD, there was an abrupt, dramatic, and steady increase in use of the CJD eponym while use of the JCD eponym remained at a low level. In the period after Gibbs ceased to publish, there was a corresponding marked fall-off in use of the CJD eponym. Surviving collaborators thought Gibbs may have been joking, but in 1991 Gibbs had admitted what Prusiner reported. Regardless of motive, Gibbs strongly influenced the preferred eponym for this human prion disease by: (1) publishing a seminal and highly referenced initial paper in a high-profile journal; (2) sustained output of further important studies published in high-quality journals over more than 30 years; (3) professional affiliation with an esteemed national laboratory where he worked with a large number of high-profile colleagues; and (4) extensive collaborations with a large number of colleagues, who published multiple further papers using the eponym Gibbs preferred.

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Weitere Beiträge zum Kapitel „Spastische Pseudosklerose Jakobs”

Cited by 24 publications

References 3 publications

Prions

Prions

Complete Genomic Sequence and Analysis of the Prion Protein Gene Region from Three Mammalian Species

Clarence J. Gibbs Effect and the “Creutzfeldt-Jakob Disease” Eponym

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