Synapse
⌘+K
Synapse
PulseExploreClubsResearchersJournals
Instagram
HomeClubsExplore
January 1, 1996Biochemistry

The Importance of the Second Hairpin Loop of Cystatin C for Proteinase Binding. Characterization of the Interaction of Trp-106 Variants of the Inhibitor with Cysteine Proteinases

View Full Paper
Ask AI
Bookmark
Share

Authors

IBIngemar BjörkSwedish University of Agricultural SciencesIBIngrid BrieditisSwedish University of Agricultural SciencesERElke Raub‐SegallSwedish University of Agricultural Sciences

Discussion

Loading...

Member takes

Implication

Key Points

Key points are not available for this paper at this time.

Cite This Study

Björk et al. (1996) studied this question.

synapsesocial.com/papers/6aa009be26b4e28929efd6f5https://doi.org/10.1021/bi960420u
View Full Paper
Ask AI
Bookmark
Share

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Probing the functional role of the N-terminal region of cystatins by equilibrium and kinetic studies of the binding of Gly-11 variants of recombinant human cystatin C to target proteinases1995 · 47 citations
  2. 2Differential changes in the association and dissociation rate constants for binding of cystatins to target proteinases occurring on N-terminal truncation of the inhibitors indicate that the interaction mechanism varies with different enzymes1994 · 85 citations
  3. 3Temporary inhibition of papain by hairpin loop mutants of chicken cystatin Distorted binding of the loops results in cleavage of the Gly9‐Ala10 bond1995 · 36 citations
  4. 4Hairpin loop mutations of chicken cystatin have different effects on the inhibition of cathepsin B, cathepsin L and papain1995 · 41 citations
  5. 5Human cathepsin H1980 · 194 citations