Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Expression of truncated phosphoproteins of Nipah virus and Hendra virus in Escherichia coli for the differentiation of henipavirus infections.

Biotechnology letters - 1 Jun 2007

Chen Ji-Ming, Yaiw Koon Chu, Yu Meng, Wang Lin-Fa, Wang Qing-Hua, Crameri Gary, Wang Zhi-Liang

Abstract excerpt

The genus Henipavirus in the family Paramyxoviridae compromises two newly identified dangerous pathogens, Nipah virus and Hendra virus. Phosphoprotein of the two viruses is one of the major immunodominant antigens and the most divergent protein in the viral genomes. We have now expressed two pairs of truncated phosphoproteins of the two viruses in Escherichia coli in a soluble form using a vector tailored from...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Blotting, Western
Share to Enzyme-Linked Immunosorbent Assay

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Gene Expression

Share to Phosphoproteins

Share to Recombinant Proteins

Share to Species Specificity

Share to Viral Proteins

Source

Identifiers

PMID: 17322967
DOI: 10.1007/s10529-007-9323-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Expression of truncated phosphoproteins of Nipah virus and Hendra virus in Escherichia coli for the differentiation of henipavirus infections.PMID 17322967Read ↗

Mapping of domains responsible for nucleocapsid protein–phosphoprotein interaction of henipavirusesSemantic proximity Read ↗

The interaction between the Nipah virus nucleocapsid protein and phosphoprotein regulates virus replicationSemantic proximity Read ↗

Determination of the henipavirus phosphoprotein gene mRNA editing frequencies and detection of the C, V and W proteins of Nipah virus in virus-infected cellsSemantic proximity Read ↗

Molecular virology of the henipaviruses.Semantic proximity Read ↗

Proteome Based Approach Defines Candidates for Designing a Multitope Vaccine against the Nipah VirusSemantic proximity Read ↗

Structure of the Nipah virus polymerase phosphoprotein complexSemantic proximity Read ↗

Screening and structure-based modeling of T-cell epitopes of Nipah virus proteome: an immunoinformatic approach for designing peptide-based vaccineSemantic proximity Read ↗

Crystal structures of Nipah and Hendra virus fusion core proteinsSemantic proximity Read ↗

Nipah virus: epidemiology, pathology, immunobiology and advances in diagnosis, vaccine designing and control strategies – a comprehensive reviewSemantic proximity Read ↗

Functional and antigenic constraints on the Nipah virus fusion proteinSemantic proximity Read ↗

The non-pathogenic Henipavirus Cedar paramyxovirus phosphoprotein has a compromised ability to target STAT1 and STAT2Semantic proximity Read ↗

Phylogeography, Transmission, and Viral Proteins of Nipah VirusSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.