LEAP‐1, a novel highly disulfide‐bonded human peptide, exhibits antimicrobial activity
By A. Krause, S. Neitz, H. Mägert, A. Schulz, W. Forssmann, P. Schulz-Knappe, K. Adermann. FEBS Letters, 2000
1,356 citations recorded by the source corpus.
Subfields: Immunology, Microbiology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/932f5f5f57b72b07cdbc5964b49ff78813e7dae0
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In Immunology
In Microbiology
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Citations in the corpus
- Historical perspective of peptidomics (2014, background): “[116] Krause A, Neitz S, Magert HJ, Schulz A, Forssmann WG, Schulz-Knappe P, et al.”
- Iron in Infection and Immunity (2013, background): “In fact, hepcidin was initially characterized as an antimicrobial peptide in human urine and blood ultrafiltrate (Krause et al., 2000; Park et al., 2001).”
- Systemic iron homeostasis. (2013, background): “7-kDa (25 amino acid) peptide (FIGURE 3) containing four disulfide bonds (132, 179, 186).”
- Hepcidin and iron regulation, 10 years later. (2011, background): “32 On the basis of the work by many groups, a model of hepcidin regulation by iron has emerged (Figure 2) in which (1) the BMP receptor and its signaling components are at the core of the regulatory mechanism and control the transcription of hepcidin thorough the Smad pathway; (2) HJV is an iron-spe”