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Cystine-Knot Miniproteins

Known as: Knottins, Cystine Knot Miniproteins, Knottin 
A structurally-related family of small proteins that form a stable tertiary fold pattern which is supported by a series of disulfide bonds. The… Expand
National Institutes of Health

Papers overview

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2012
2012
Antibodies have been widely used in a range of biopharmaceutical and biomedical applications due to their intrinsic high affinity… Expand
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Highly Cited
2010
Highly Cited
2010
Targeted contrast-enhanced ultrasound imaging is increasingly being recognized as a powerful imaging tool for the detection and… Expand
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Highly Cited
2010
Highly Cited
2010
Here we report the design, chemical and recombinant synthesis, and functional properties of a series of novel inhibitors of human… Expand
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Highly Cited
2009
Highly Cited
2009
There is a critical need for compounds that target cell surface integrin receptors for applications in cancer therapy and… Expand
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Review
2009
Review
2009
  • Harald Kolmar
  • Current opinion in pharmacology
  • 2009
  • Corpus ID: 5253009
Owing to their outstanding inherent thermal stability and proteolytic resistance, as well as their small size of only around 30… Expand
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Highly Cited
2009
Highly Cited
2009
Hydramacin-1 is a novel antimicrobial protein recently discovered during investigations of the epithelial defense of the ancient… Expand
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Highly Cited
2008
Highly Cited
2008
The KNOTTIN database provides standardized information on the small disulfide-rich proteins with a knotted topology called… Expand
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Highly Cited
2005
Highly Cited
2005
From seeds of Triticum kiharae Dorof. et Migusch., 24 novel anti-microbial peptides were isolated and characterized by a… Expand
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Highly Cited
2001
Highly Cited
2001
The "knottin" fold is a stable cysteine-rich scaffold, in which one disulfide crosses the macrocycle made by two other disulfides… Expand
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Review
1998
Review
1998
Eight families of antimicrobial peptides, ranging in size from 2 to 9 kD, have been identified in plants. These are thionins… Expand
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