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Relationships among serum cystatin C, serum creatinine, lean tissue mass and glomerular filtration rate in healthy adults.
Vinge E, Lindergård B, Nilsson-Ehle P, Grubb A. Vinge E, et al. Scand J Clin Lab Invest. 1999 Dec;59(8):587-92. doi: 10.1080/00365519950185076. Scand J Clin Lab Invest. 1999. PMID: 10691049
In an effort to increase our knowledge of the optimal use of serum cystatin C and creatinine as glomerular filtration rate (GFR) markers, these variables, as well as lean tissue mass and GFR, were determined in a population of 42 healthy young adults (men and women with no …
In an effort to increase our knowledge of the optimal use of serum cystatin C and creatinine as glomerular filtration rate (GFR) markers, th …
Diagnostic value of analysis of cystatin C and protein HC in biological fluids.
Grubb A. Grubb A. Clin Nephrol. 1992;38 Suppl 1:S20-7. Clin Nephrol. 1992. PMID: 1284235 Review.
Cystatin C, a 13 kDa-protein, is produced by most nucleated cells and is catabolized by the renal tubular cells after passing the glomerular filter. ...Protein HC, alias alpha 1-microglobulin, is produced by the liver as a 27 kDa-glycoprotein. It belongs to the lipo …
Cystatin C, a 13 kDa-protein, is produced by most nucleated cells and is catabolized by the renal tubular cells after passing the glo …
Cystatin C based peptidyl diazomethanes as cysteine proteinase inhibitors: influence of the peptidyl chain length.
Hall A, Abrahamson M, Grubb A, Trojnar J, Kania P, Kasprzykowska R, Kasprzykowski F. Hall A, et al. J Enzyme Inhib. 1992;6(2):113-23. doi: 10.3109/14756369209040742. J Enzyme Inhib. 1992. PMID: 1284427
These data suggest that the arginyl residue of the tetrapeptidyl diazomethane, and also the corresponding arginyl residue in native cystatin C, interact with a S4 substrate pocket subsite of both papain and cathepsin B. ...
These data suggest that the arginyl residue of the tetrapeptidyl diazomethane, and also the corresponding arginyl residue in native cystatin …
Hereditary cystatin C amyloid angiopathy: identification of the disease-causing mutation and specific diagnosis by polymerase chain reaction based analysis.
Abrahamson M, Jonsdottir S, Olafsson I, Jensson O, Grubb A. Abrahamson M, et al. Hum Genet. 1992 Jun;89(4):377-80. doi: 10.1007/BF00194306. Hum Genet. 1992. PMID: 1352269
A method for rapid and simple diagnosis of HCCAA is described. It is based upon oligonucleotide-directed enzymatic amplification of a 275-bp genomic DNA segment containing exon 2 of the cystatin C gene from a blood sample, followed by digestion of the amplifi
A method for rapid and simple diagnosis of HCCAA is described. It is based upon oligonucleotide-directed enzymatic amplification of
Microcalorimetric studies on uraemic plasma.
Ljunggren L, Monti M, Thysell H, Grubb A. Ljunggren L, et al. Scand J Clin Lab Invest. 1992 Dec;52(8):813-7. doi: 10.3109/00365519209088385. Scand J Clin Lab Invest. 1992. PMID: 1488619
Demonstration of sequence variations in the promoter region of the human cystatin C gene.
Balbin M, Grubb A, Abrahamson M. Balbin M, et al. Biol Chem Hoppe Seyler. 1992 Jul;373(7):471-6. doi: 10.1515/bchm3.1992.373.2.471. Biol Chem Hoppe Seyler. 1992. PMID: 1515077
Two of the observed mutations are involved in a novel Sst II polymorphism and another generates a new Dde I restriction site. A PCR-based assay for analysis of these Sst II and Dde I sites was designed and used to demonstrate Mendelian inheritance of the poly …
Two of the observed mutations are involved in a novel Sst II polymorphism and another generates a new Dde I restriction site. …
Regulation of cystatin C activity by serine proteinases.
Abrahamson M, Buttle DJ, Mason RW, Hansson H, Grubb A, Lilja H, Ohlsson K. Abrahamson M, et al. Biomed Biochim Acta. 1991;50(4-6):587-93. Biomed Biochim Acta. 1991. PMID: 1801727
Neutrophil elastase in catalytic amounts was observed to rapidly cleave cystatin C at neutral pH, thereby giving rise to a modified form of the inhibitor lacking the N-terminal Ser1-Val10 decapeptide. ...
Neutrophil elastase in catalytic amounts was observed to rapidly cleave cystatin C at neutral pH, thereby giving rise to a modified f …
Human cystatin C. role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase.
Abrahamson M, Mason RW, Hansson H, Buttle DJ, Grubb A, Ohlsson K. Abrahamson M, et al. Biochem J. 1991 Feb 1;273 ( Pt 3)(Pt 3):621-6. doi: 10.1042/bj2730621. Biochem J. 1991. PMID: 1996959 Free PMC article.
A tripeptidyldiazomethane analogue of of the N-terminal portion of cystatin C was a good inhibitor of cathepsins B and L but a poor inhibitor of cathepsin H. ...It is argued that the N-terminal cystatin C interaction with cathepsin B is physiologically import
A tripeptidyldiazomethane analogue of of the N-terminal portion of cystatin C was a good inhibitor of cathepsins B and L but
Cystatin C, a human proteinase inhibitor, blocks replication of herpes simplex virus.
Björck L, Grubb A, Kjellén L. Björck L, et al. J Virol. 1990 Feb;64(2):941-3. doi: 10.1128/JVI.64.2.941-943.1990. J Virol. 1990. PMID: 2153254 Free PMC article.
Cystatin C is a human cysteine proteinase inhibitor present in extracellular fluids. Cystatin C and a tripeptide derivative (Z-LVG-CHN2) that mimics its proteinase-binding center, were tested for possible antiviral activity against herpes simplex virus type 1 (HSV) …
Cystatin C is a human cysteine proteinase inhibitor present in extracellular fluids. Cystatin C and a tripeptide derivative (Z …
The amino terminal portion of cerebrospinal fluid cystatin C in hereditary cystatin C amyloid angiopathy is not truncated: direct sequence analysis from agarose gel electropherograms.
Olafsson I, Gudmundsson G, Abrahamson M, Jensson O, Grubb A. Olafsson I, et al. Scand J Clin Lab Invest. 1990 Feb;50(1):85-93. doi: 10.1080/00365519009091569. Scand J Clin Lab Invest. 1990. PMID: 2315647
The isolated amyloid substance in hereditary cystatin C amyloid angiopathy (HCCAA) is mainly composed of a cystatin C variant devoid of the 10 amino terminal amino acid residues of extracellular cystatin C from healthy individuals. ...The amino-terminal sequence determined …
The isolated amyloid substance in hereditary cystatin C amyloid angiopathy (HCCAA) is mainly composed of a cystatin C variant devoid …
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