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rdf:type |
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lifeskim:mentions |
umls-concept:C0007637,
umls-concept:C0017262,
umls-concept:C0021027,
umls-concept:C0185117,
umls-concept:C0525009,
umls-concept:C1280500,
umls-concept:C1514562,
umls-concept:C1522492,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2911684
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pubmed:issue |
2
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pubmed:dateCreated |
1997-4-25
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pubmed:abstractText |
Inclusion body (IB) formation in bacteria is an important example of protein misassembly, a phenomenon which also includes folding-dependent aggregation in vitro and amyloid deposition in human disease. Previous studies of mutational effects in other systems implicate the stability of a folding intermediate-rather than the native state-as playing a key role in IB formation. To contribute to an understanding of the comparative biophysics of VL misassembly in different biological settings, we have studied mutation-dependent periplasmic IB formation by the VL domain REI in Escherichia coli.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1359-0278
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
77-89
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:9079368-Amino Acid Sequence,
pubmed-meshheading:9079368-Base Sequence,
pubmed-meshheading:9079368-DNA, Recombinant,
pubmed-meshheading:9079368-Dimerization,
pubmed-meshheading:9079368-Drug Stability,
pubmed-meshheading:9079368-Escherichia coli,
pubmed-meshheading:9079368-Gene Expression,
pubmed-meshheading:9079368-Humans,
pubmed-meshheading:9079368-Immunoglobulin Light Chains,
pubmed-meshheading:9079368-Immunoglobulin Variable Region,
pubmed-meshheading:9079368-Inclusion Bodies,
pubmed-meshheading:9079368-Microscopy, Electron,
pubmed-meshheading:9079368-Models, Molecular,
pubmed-meshheading:9079368-Molecular Sequence Data,
pubmed-meshheading:9079368-Molecular Structure,
pubmed-meshheading:9079368-Mutation,
pubmed-meshheading:9079368-Peptide Fragments,
pubmed-meshheading:9079368-Protein Conformation,
pubmed-meshheading:9079368-Protein Folding,
pubmed-meshheading:9079368-Recombinant Proteins,
pubmed-meshheading:9079368-Solubility,
pubmed-meshheading:9079368-Thermodynamics
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pubmed:year |
1996
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pubmed:articleTitle |
Mutational effects on inclusion body formation in the periplasmic expression of the immunoglobulin VL domain REI.
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pubmed:affiliation |
Department of Macromolecular Sciences, SmithKline Beecham Pharmaceuticals, King of Prussia, PA 19406, USA.
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pubmed:publicationType |
Journal Article
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