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Anders Grubb

Researcher at Lund University

Publications -  365
Citations -  24247

Anders Grubb is an academic researcher from Lund University. The author has contributed to research in topics: Cystatin C & Renal function. The author has an hindex of 79, co-authored 353 publications receiving 22712 citations. Previous affiliations of Anders Grubb include University of Copenhagen & State University of New York System.

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Serum cystatin C measured by automated immunoassay: A more sensitive marker of changes in GFR than serum creatinine

TL;DR: Cystatin C measurement using PETIA technology can be automated on the same instruments used routinely for the measurement of creatinine and offers better analytical performance and probably improved clinical sensitivity as a screening test for early renal damage.
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Cystatin C as a marker of GFR--history, indications, and future research.

TL;DR: A multinational expert meeting was held in April 2002 in Marburg, Germany as discussed by the authors to summarize recent knowledge on the protein cystatin C (cys-C) and its use as a marker of the glomerular filtration rate (GFR).
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Structure and expression of the human cystatin C gene.

TL;DR: The apparently non-tissue-specific expression of this cysteine-proteinase inhibitor gene is discussed with respect to the structure of its 5'-flanking region, which shares several features with those of housekeeping genes.
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Serum cystatin C, determined by a rapid, automated particle-enhanced turbidimetric method, is a better marker than serum creatinine for glomerular filtration rate.

TL;DR: A fully automated particle-enhanced turbidimetric assay for cystatin C in undiluted serum and EDTA-plasma that seems an attractive alternative to creatinine for estimation of GFR.
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Isolation of six cysteine proteinase inhibitors from human urine. Their physicochemical and enzyme kinetic properties and concentrations in biological fluids

TL;DR: The combined enzyme kinetic and concentration data showed that several of the inhibitors have the capacity to play physiologically important roles as cysteine proteinase inhibitors in many biological fluids.