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Literature DB >> 8520469

The picornaviral 3C proteinases: cysteine nucleophiles in serine proteinase folds.

Abstract

The 3C proteinases are a novel group of cysteine proteinases with a serine proteinase-like fold that are responsible for the bulk of polyprotein processing in the Picornaviridae. Because members of this viral family are to blame for several ongoing global pandemic problems (rhinovirus, hepatitis A virus) as well as sporadic outbreaks of more serious pathologies (poliovirus), there has been continuing interest over the last two decades in the development of antiviral therapies. The recent determination of the structure of two of the 3C proteinases by X-ray crystallography opens the door for the application of the latest advances in computer-assisted identification and design of anti-proteinase therapeutic/chemoprophylactic agents.

Entities: Gene Species

Mesh：

Substances：

Year: 1995 PMID： 8520469 PMCID： PMC2143194 DOI： 10.1002/pro.5560040801

Source DB: PubMed Journal: Protein Sci ISSN： 0961-8368 Impact factor: 6.725

48 in total

1. Intermolecular cleavage of hepatitis A virus (HAV) precursor protein P1-P2 by recombinant HAV proteinase 3C.

Authors: Y Y Kusov; W Sommergruber; M Schreiber; V Gauss-Müller
Journal: J Virol Date: 1992-11 Impact factor: 5.103

Review 2. How do serine proteases really work?

Authors: A Warshel; G Naray-Szabo; F Sussman; J K Hwang
Journal: Biochemistry Date: 1989-05-02 Impact factor: 3.162

Review 3. Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. A distinct protein superfamily with a common structural fold.

Authors: A E Gorbalenya; A P Donchenko; V M Blinov; E V Koonin
Journal: FEBS Lett Date: 1989-01-30 Impact factor: 4.124

4. Cleavage of synthetic peptides by purified poliovirus 3C proteinase.

Authors: P V Pallai; F Burkhardt; M Skoog; K Schreiner; P Bax; K A Cohen; G Hansen; D E Palladino; K S Harris; M J Nicklin
Journal: J Biol Chem Date: 1989-06-15 Impact factor: 5.157

5. Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses.

Authors: J F Bazan; R J Fletterick
Journal: Virology Date: 1989-08 Impact factor: 3.616

6. Chimeric picornavirus polyproteins demonstrate a common 3C proteinase substrate specificity.

Authors: P G Dewalt; M A Lawson; R J Colonno; B L Semler
Journal: J Virol Date: 1989-08 Impact factor: 5.103

7. Polypeptide 2A of human rhinovirus type 2: identification as a protease and characterization by mutational analysis.

Authors: W Sommergruber; M Zorn; D Blaas; F Fessl; P Volkmann; I Maurer-Fogy; P Pallai; V Merluzzi; M Matteo; T Skern
Journal: Virology Date: 1989-03 Impact factor: 3.616

8. A rapid method for determination of endoproteinase substrate specificity: specificity of the 3C proteinase from hepatitis A virus.

Authors: J R Petithory; F R Masiarz; J F Kirsch; D V Santi; B A Malcolm
Journal: Proc Natl Acad Sci U S A Date: 1991-12-15 Impact factor: 11.205

9. Polyprotein processing in cis and in trans by hepatitis A virus 3C protease cloned and expressed in Escherichia coli.

Authors: S A Harmon; W Updike; X Y Jia; D F Summers; E Ehrenfeld
Journal: J Virol Date: 1992-09 Impact factor: 5.103

10. Expression and characterization of recombinant hepatitis A virus 3C proteinase.

Authors: B A Malcolm; S M Chin; D A Jewell; J R Stratton-Thomas; K B Thudium; R Ralston; S Rosenberg
Journal: Biochemistry Date: 1992-04-07 Impact factor: 3.162

28 in total

1. Nitric oxide inhibition of coxsackievirus replication in vitro.

Authors: C Zaragoza; C J Ocampo; M Saura; A McMillan; C J Lowenstein
Journal: J Clin Invest Date: 1997-10-01 Impact factor: 14.808

2. The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition.

Authors: E M Bergmann; S C Mosimann; M M Chernaia; B A Malcolm; M N James
Journal: J Virol Date: 1997-03 Impact factor: 5.103

Review 3. Problems and prospects of developing effective therapy for common cold viruses.

Authors: S L Johnston
Journal: Trends Microbiol Date: 1997-02 Impact factor: 17.079

4. The enterovirus 3C protease inhibitor SG85 efficiently blocks rhinovirus replication and is not cross-resistant with rupintrivir.

Authors: Céline Lacroix; Shyla George; Pieter Leyssen; Rolf Hilgenfeld; Johan Neyts
Journal: Antimicrob Agents Chemother Date: 2015-06-08 Impact factor: 5.191