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cystatin, egg-white

Known as: chicken cystatin, cystatin (desSer1, Ile29, Leu89), egg-white cystatin 
National Institutes of Health

Related topics

Related topics

2 relations

Broader (2)

CystatinsCysteine Proteinase Inhibitors

Papers overview

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Highly Cited
2004
Highly Cited
2004
Cystatin forms a tetramer through structural rearrangement of domain-swapped dimers prior to amyloidogenesis.
The cystatins were the first amyloidogenic proteins to be shown to oligomerize through a 3D domain swapping mechanism. Here we… Expand
Highly Cited
2001
Highly Cited
2001
Three‐dimensional domain swapping in the folded and molten‐globule states of cystatins, an amyloid‐forming structural superfamily
Cystatins, an amyloid‐forming structural superfamily, form highly stable, domain‐swapped dimers at physiological protein… Expand
Highly Cited
2000
Highly Cited
2000
Cysteine proteinase inhibitors stefin A, stefin B, and cystatin C in sera from patients with colorectal cancer: relation to prognosis.
The levels of cysteine proteinase inhibitors stefin A, stefin B, and cystatin C were determined using ELISAs in sera obtained… Expand
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Highly Cited
1997
Highly Cited
1997
NMR structural studies of human cystatin C dimers and monomers.
Human cystatin C undergoes dimerization before unfolding. Dimerization leads to a complete loss of its activity as a cysteine… Expand
Highly Cited
1996
Highly Cited
1996
Cystatins Up-regulate Nitric Oxide Release from Interferon-γ- activated Mouse Peritoneal Macrophages*
  • Ludovic Verdot, Gilles Lalmanach, +5 authors Bernard Vray
  • The Journal of Biological Chemistry
  • 1996
    • Corpus ID: 9787253
Up-regulation of nitric oxide (NO) production by activated murine macrophages was observed during infection by Trypanosoma cruzi… Expand
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Highly Cited
1993
Highly Cited
1993
The two cysteine endopeptidases of legume seeds: purification and characterization by use of specific fluorometric assays.
Two endopeptidases are present in the seeds of Vigna aconitifolia (moth bean), and their activities increase during germination… Expand
Highly Cited
1993
Highly Cited
1993
Kinetics of the pH-induced inactivation of human cathepsin L.
Cathepsin L is known as the most unstable lysosomal cysteine proteinase at neutral or alkaline pH. The kinetics of inactivation… Expand
Review
1991
Review
1991
The cystatins: Protein inhibitors of cysteine proteinases
  • Vito Turk, W. Bode
  • FEBS letters
  • 1991
    • Corpus ID: 40444629
The last decade has witnessed enormous progress of protein inhibitors of cysteine proteinases concerning their structures… Expand
Highly Cited
1987
Highly Cited
1987
Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors human cystatin C and chicken cystatin.
When an excess of human cystatin C or chicken cystatin was mixed with papain, an enzyme-inhibitor complex was formed immediately… Expand
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Highly Cited
1986
Highly Cited
1986
Nomenclature and classification of the proteins homologous with the cysteine-proteinase inhibitor chicken cystatin.
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