(Q27469528)

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Signal peptidase cleavage at the flavivirus C-prM junction: dependence on the viral NS2B-3 protease for efficient processing requires determinants in C, the signal peptide, and prM

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Europe PubMed Central

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10 November 2019

Signal peptidase cleavage at the flavivirus C-prM junction: dependence on the viral NS2B-3 protease for efficient processing requires determinants in C, the signal peptide, and prM (English)

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9499070%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

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Stocks CE

1

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10 November 2019

Lobigs M

2

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10 November 2019

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1 March 1998

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10 November 2019

Journal of Virology

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10 November 2019

72

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10 November 2019

3

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10 November 2019

2141-2149

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10 November 2019

NS2B-3 proteinase-mediated processing in the yellow fever virus structural region: in vitro and in vivo studies

1 reference

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21 March 2017

Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro

1 reference

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21 March 2017

Processing of yellow fever virus polyprotein: role of cellular proteases in maturation of the structural proteins

1 reference

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Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma

1 reference

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Nucleotide sequence of yellow fever virus: implications for flavivirus gene expression and evolution

1 reference

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21 March 2017

A new method for predicting signal sequence cleavage sites

1 reference

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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Post-translational protein translocation: not all hsc70s are created equal

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Flavivirus premembrane protein cleavage and spike heterodimer secretion require the function of the viral proteinase NS3.

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The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase

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Can Hsp70 proteins act as force-generating motors?

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Polypeptide requirements for assembly of functional Sindbis virus replication complexes: a model for the temporal regulation of minus- and plus-strand RNA synthesis

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A cDNA clone containing the entire coding sequence of a mouse H-2Kd histocompatibility antigen

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Dengue 2 Virus Envelope Protein Expressed by a Recombinant Vaccinia Virus Fails to Protect Monkeys against Dengue

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Proteases involved in the processing of viral polyproteins. Brief review

1 reference

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29 September 2017

Viral proteinases

1 reference

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29 September 2017

Partial nucleotide sequence of the Murray Valley encephalitis virus genome. Comparison of the encoded polypeptides with yellow fever virus structural and non-structural proteins

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29 September 2017

Sequence analysis of the viral core protein and the membrane-associated proteins V1 and NV2 of the flavivirus West Nile virus and of the genome sequence for these proteins

1 reference

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Nucleotide sequence of dengue 2 RNA and comparison of the encoded proteins with those of other flaviviruses

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Proteolytic processing of polyproteins in the replication of RNA viruses

1 reference

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Proteolytic processing of picornaviral polyprotein

1 reference

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Function of Semliki Forest virus E3 peptide in virus assembly: replacement of E3 with an artificial signal peptide abolishes spike heterodimerization and surface expression of E1.

1 reference

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The signal peptide

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=109509

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Cleavage-site preferences of Sindbis virus polyproteins containing the non-structural proteinase. Evidence for temporal regulation of polyprotein processing in vivo

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Recombinant vaccinia virus producing the prM and E proteins of yellow fever virus protects mice from lethal yellow fever encephalitis

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Epitope Analysis of the Envelope and Non-structural Glycoproteins of Murray Valley Encephalitis Virus

1 reference

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Ubiquitin as a degradation signal

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Complete nucleotide sequence of the Japanese encephalitis virus genome RNA.

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Single amino acid substitutions can convert the uncleaved signal-anchor of sucrase-isomaltase to a cleaved signal sequence.

1 reference

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1 reference

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Are transporter associated with antigen processing (TAP) and tapasin class I MHC chaperones?

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Eukaryotic signal peptide structure/function relationships. Identification of conformational features which influence the site and efficiency of co-translational proteolytic processing by site-directed mutagenesis of human pre(delta pro)apolipoprote

1 reference

https://pubmed.ncbi.nlm.nih.gov/9499070

12 December 2020

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Identifiers

10.1128/JVI.72.3.2141-2149.1998

0 references

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9499070%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9499070%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

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