"Aprotinin" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A single-chain polypeptide derived from bovine tissues consisting of 58 amino-acid residues. It is an inhibitor of proteolytic enzymes including CHYMOTRYPSIN; KALLIKREIN; PLASMIN; and TRYPSIN. It is used in the treatment of HEMORRHAGE associated with raised plasma concentrations of plasmin. It is also used to reduce blood loss and transfusion requirements in patients at high risk of major blood loss during and following open heart surgery with EXTRACORPOREAL CIRCULATION. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995)
- Trypsin Inhibitor, Basic, Pancreatic
- Bovine Kunitz Pancreatic Trypsin Inhibitor
- BPTI, Basic Pancreatic Trypsin Inhibitor
- Kallikrein-Trypsin Inactivator
- Inactivator, Kallikrein-Trypsin
- Kallikrein Trypsin Inactivator
- Kunitz Pancreatic Trypsin Inhibitor
- Trypsin Inhibitor, Kunitz, Pancreatic
- Basic Pancreatic Trypsin Inhibitor
- Bovine Pancreatic Trypsin Inhibitor
Below are MeSH descriptors whose meaning is more general than "Aprotinin".
Below are MeSH descriptors whose meaning is more specific than "Aprotinin".
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Below are the most recent publications written about "Aprotinin" by people in Profiles.
Lin KH, Ali A, Rusere L, Soumana DI, Kurt Yilmaz N, Schiffer CA. Dengue Virus NS2B/NS3 Protease Inhibitors Exploiting the Prime Side. J Virol. 2017 05 15; 91(10).
Zhou HX, Bilsel O. SAXS/SANS probe of intermolecular interactions in concentrated protein solutions. Biophys J. 2014 Feb 18; 106(4):771-3.
Raghunathan K, Connelly NR, Kanter GJ. e-Aminocaproic acid and clinical value in cardiac anesthesia. J Cardiothorac Vasc Anesth. 2011 Feb; 25(1):16-9.
Habib RH, Zacharias A, Schwann TA. Long-term mortality associated with aprotinin following coronary artery bypass graft surgery. JAMA. 2007 Jun 13; 297(22):2476-7; author reply 2477.
Massi F, Johnson E, Wang C, Rance M, Palmer AG. NMR R1 rho rotating-frame relaxation with weak radio frequency fields. J Am Chem Soc. 2004 Feb 25; 126(7):2247-56.
Schiffer CA, van Gunsteren WF. Accessibility and order of water sites in and around proteins: A crystallographic time-averaging study. Proteins. 1999 Sep 01; 36(4):501-11.
Schiffer CA, van Gunsteren WF. Structural stability of disulfide mutants of basic pancreatic trypsin inhibitor: a molecular dynamics study. Proteins. 1996 Sep; 26(1):66-71.
Schiffer CA, Huber R, W?thrich K, van Gunsteren WF. Simultaneous refinement of the structure of BPTI against NMR data measured in solution and X-ray diffraction data measured in single crystals. J Mol Biol. 1994 Aug 26; 241(4):588-99.
van Gunsteren WF, Brunne RM, Gros P, van Schaik RC, Schiffer CA, Torda AE. Accounting for molecular mobility in structure determination based on nuclear magnetic resonance spectroscopic and X-ray diffraction data. Methods Enzymol. 1994; 239:619-54.
Lilly CM, Martins MA, Drazen JM. Peptidase modulation of vasoactive intestinal peptide pulmonary relaxation in tracheal superfused guinea pig lungs. J Clin Invest. 1993 Jan; 91(1):235-43.