(Q28368170)

2

0 references

K Abe

3

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M Kuroda

4

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S Arai

5

0 references

R Okamura

6

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A Negi

7

0 references

H Maeda

Antimicrobial Agents and Chemotherapy

8

0 references

language of work or name

English

0 references

publication date

April 1995

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published in

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volume

39

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issue

4

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page(s)

846-9

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cites work

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Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). Homology with animal cystatins and transient expression in the ripening process of rice seeds

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The herpes simplex virus 1 gene encoding a protease also contains within its coding domain the gene encoding the more abundant substrate

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Corn kernel cysteine proteinase inhibitor as a novel cystatin superfamily member of plant origin. Molecular cloning and expression studies

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Herpes simplex virus type 1 protease expressed in Escherichia coli exhibits autoprocessing and specific cleavage of the ICP35 assembly protein

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Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases. Molecular cloning, expression, and biochemical studies on oryzacystatin-II.

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Processing of the herpes simplex virus assembly protein ICP35 near its carboxy terminal end requires the product of the whole of the UL26 reading frame

2 June 2018

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Purification of active herpes simplex virus-1 protease expressed in Escherichia coli

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A detergent-soluble extract of virus-infected cells free from infectious virus protects mice from lethal herpes simplex virus infection.

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