Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method (Q27653406)

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Language	Label	Description	Also known as
English	Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method	scientific article

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scholarly article

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Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method (English)

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Fuyuhiko Inagaki

4

object named as

Fuyuhiko Inagaki

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author name string

Yoshihiro Kobashigawa

1

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Hiroyuki Kumeta

2

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Kenji Ogura

3

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language of work or name

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publication date

March 2009

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Journal of Biomolecular NMR

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43

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3

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145-50

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Intein-based biosynthetic incorporation of unlabeled protein tags into isotopically labeled proteins for NMR studies.

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https://pubmed.ncbi.nlm.nih.gov/19140010

12 December 2020

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A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins.

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https://pubmed.ncbi.nlm.nih.gov/19140010

12 December 2020

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Solution structure of the ubiquitin-associated domain of human BMSC-UbP and its complex with ubiquitin

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https://pubmed.ncbi.nlm.nih.gov/19140010

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Autoregulation of a bacterial sigma factor explored by using segmental isotopic labeling and NMR

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https://pubmed.ncbi.nlm.nih.gov/19140010

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Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK

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https://pubmed.ncbi.nlm.nih.gov/19140010

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Sortase: the surface protein anchoring transpeptidase and the LPXTG motif

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https://pubmed.ncbi.nlm.nih.gov/19140010

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NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain

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https://pubmed.ncbi.nlm.nih.gov/19140010

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Synthesis of adenoviral targeting molecules by intein-mediated protein ligation

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A disease state mutation unfolds the parkin ubiquitin-like domain.

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An efficient method for protein phosphorylation using the artificially introduced of cognate-binding modules into kinases and substrates

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Anchoring of surface proteins to the cell wall of Staphylococcus aureus. III. Lipid II is an in vivo peptidoglycan substrate for sortase-catalyzed surface protein anchoring

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https://pubmed.ncbi.nlm.nih.gov/19140010

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Overexpression of post-translationally modified peptides in Escherichia coli by co-expression with modifying enzymes

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https://pubmed.ncbi.nlm.nih.gov/19140010

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Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR

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https://pubmed.ncbi.nlm.nih.gov/19140010

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Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall

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https://pubmed.ncbi.nlm.nih.gov/19140010

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Chemical ligation of folded recombinant proteins: segmental isotopic labeling of domains for NMR studies

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https://pubmed.ncbi.nlm.nih.gov/19140010

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The button test: a small scale method using microdialysis cells for assessing protein solubility at concentrations suitable for NMR

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https://pubmed.ncbi.nlm.nih.gov/19140010

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A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G

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https://pubmed.ncbi.nlm.nih.gov/19140010

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Protein ligation: an enabling technology for the biophysical analysis of proteins

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https://pubmed.ncbi.nlm.nih.gov/19140010

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Sortase-mediated protein ligation: a new method for protein engineering

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https://pubmed.ncbi.nlm.nih.gov/19140010

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Improved segmental isotope labeling of proteins and application to a larger protein

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https://pubmed.ncbi.nlm.nih.gov/19140010

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10.1007/S10858-008-9296-5

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