Glycosylation and NH2-terminal domain mutants of the tissue inhibitor of metalloproteinases-1 (TIMP-1).

doi:10.1016/s0167-4838(98)00158-7

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Article

Glycosylation and NH2-terminal domain mutants of the tissue inhibitor of metalloproteinases-1 (TIMP-1).

Biochimica et biophysica acta - 14 Oct 1998

Caterina N C, Windsor L J, Bodden M K, Yermovsky A E, Taylor K B, Birkedal-Hansen H, Engler J A

Abstract excerpt

Mutants in the tissue inhibitor of metalloproteinases-1 (TIMP-1) protein have been created by site-directed mutagenesis and expressed in HeLa cells, using a recombinant vaccinia virus system. Removal of either or both glycosylation sites yielded proteins which retained wild-type inhibitory activi...

Topics

Amino Acid Sequence
Conserved Sequence
Glycosylation
HeLa Cells
Humans
Molecular Sequence Data
Molecular Weight
Mutagenesis, Site-Directed
Mutation
Recombinant Proteins
Sequence Deletion
Tissue Inhibitor of Metalloproteinase-1
Vaccinia virus

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PMID: 9774703
DOI: 10.1016/s0167-4838(98)00158-7

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9774703-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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