Proteolysis of abnormal prion protein with a thermostable protease from Thermococcus kodakarensis KOD1. (Q42253928)

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5 March 2020

title

Proteolysis of abnormal prion protein with a thermostable protease from Thermococcus kodakarensis KOD1 (English)

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5 March 2020

0 references

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Thermococcus kodakarensis

object named as

Thermococcus kodakarensis

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Yuichi Koga

1

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5 March 2020

Shun-ichi Tanaka

2

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5 March 2020

Akikazu Sakudo

3

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5 March 2020

Minoru Tobiume

4

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5 March 2020

Mutsuo Aranishi

5

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5 March 2020

Azumi Hirata

6

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5 March 2020

Kazuyoshi Ikuta

8

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5 March 2020

language of work or name

English

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publication date

24 July 2013

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Applied Microbiology and Biotechnology

5 March 2020

published in

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5 March 2020

volume

98

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5 March 2020

issue

5

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5 March 2020

page(s)

2113-2120

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Activity of an alkaline 'cleaner' in the inactivation of the scrapie agent

5 March 2020

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An enzyme-detergent method for effective prion decontamination of surgical steel.

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Active subtilisin-like protease from a hyperthermophilic archaeon in a form with a putative prosequence

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Decontamination of surgical instruments from prions. II. In vivo findings with a model system for testing the removal of scrapie infectivity from steel surfaces

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A protease-resistant protein is a structural component of the scrapie prion

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Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins

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Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient

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Ca2+-dependent maturation of subtilisin from a hyperthermophilic archaeon, Thermococcus kodakaraensis: the propeptide is a potent inhibitor of the mature domain but is not required for its folding

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Crystal structure of unautoprocessed precursor of subtilisin from a hyperthermophilic archaeon: evidence for Ca2+-induced folding

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The physical relationship between infectivity and prion protein aggregates is strain-dependent

21 January 2018

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Generating a prion with bacterially expressed recombinant prion protein

21 January 2018

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