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- aggregation classification "A1".
- aggregation creator B157070.
- aggregation creator B157071.
- aggregation creator B157072.
- aggregation creator B157073.
- aggregation creator person.
- aggregation date "2004".
- aggregation format "application/pdf".
- aggregation hasFormat 298938.bibtex.
- aggregation hasFormat 298938.csv.
- aggregation hasFormat 298938.dc.
- aggregation hasFormat 298938.didl.
- aggregation hasFormat 298938.doc.
- aggregation hasFormat 298938.json.
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- aggregation hasFormat 298938.yaml.
- aggregation isPartOf urn:issn:0031-949X.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Interaction between tomato spotted wilt virus N protein monomers involves nonelectrostatic forces governed by multiple distinct regions in the primary structure".
- aggregation abstract "The ambisense RNA genome of Tomato spotted wilt virus (TSWV) is packaged by interaction with numerous copies of the virus encoded nucleocapsid (N) protein to form a subvirion structure called a ribonucleoprotein (RNP). RNPs are central to the viral replication cycle because they, and not free viral RNA, serve as templates for viral gene expression and genome replication. N protein monomers bind to viral RNA molecules in a cooperative manner. We have examined regions of the N protein that are involved in the N-N interactions that likely contribute to the cooperative binding of N to viral RNA. We created random and alanine scanning mutants of N and then screened the mutants for defects in N-N interaction using reverse and forward yeast two-hybrid assays. Our experiments identified residues in three distinct regions of the primary structure of the protein, residues 42 to 56, 132 to 152, and in the C-terminal 26 amino acids, that contribute to N-N dimerization or multimerization. The interactions between N monomers mediated by the residues we identified are of a nonelectrostatic nature.".
- aggregation authorList BK391738.
- aggregation endPage "765".
- aggregation issue "7".
- aggregation startPage "759".
- aggregation volume "94".
- aggregation aggregates 4141254.
- aggregation isDescribedBy 298938.
- aggregation similarTo PHYTO.2004.94.7.759.
- aggregation similarTo LU-298938.