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cystatin, egg-white

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

Papers overview

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Highly Cited
2004
Highly Cited
2004
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
Cystatins, an amyloid‐forming structural superfamily, form highly stable, domain‐swapped dimers at physiological protein… Expand
Highly Cited
2000
Highly Cited
2000
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
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
  • 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
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
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
  • 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
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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