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The structural basis for autoinhibition of FLT3 by the juxtamembrane domain.
FLT3 is a type III receptor tyrosine kinase that is thought to play a key role in hematopoiesis. Certain classes of FLT3 mutations cause constitutively activated forms of the receptor that are foundExpand
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An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase.
Electrostatic calculations based on the recently solved crystal structure of acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) indicate that this enzyme has a strong electrostaticExpand
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Open "back door" in a molecular dynamics simulation of acetylcholinesterase.
The enzyme acetylcholinesterase generates a strong electrostatic field that can attract the cationic substrate acetylcholine to the active site. However, the long and narrow active site gorge seemsExpand
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Trypanocidal bisbenzylisoquinoline alkaloids are inhibitors of trypanothione reductase.
Eleven bisbenzylisoquinoline (BBIQ) alkaloids were studied for in vitro trypanocidal activity against trypomastigote forms of the Y strain of Trypanosoma cruzi. The inhibitory activity of theseExpand
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Backbone makes a significant contribution to the electrostatics of α/β‐barrel proteins
The electrostatic properties of seven α/β‐barrel enzymes selected from different evolutionary families were studied: triose phosphate isomerase, fructose‐1,6‐bisphosphate aldolase, pyruvate kinase,Expand
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Kukoamine A and other hydrophobic acylpolyamines: potent and selective inhibitors of Crithidia fasciculata trypanothione reductase.
The enzyme trypanothione reductase (TR), together with its substrate, the glutathione-spermidine conjugate trypanothione, plays an essential role in protecting parasitic trypanosomatids againstExpand
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Consensus preferred hydration sites in six FKBP12‐drug complexes
A set of consens us hydration sites for the FK506‐FKBP12 complex are derived by comparing six FKBP12‐drug complexes. These hydration sites include a subset of the observed water molecules plus someExpand
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Cooperativity of papain-substrate interaction energies in the S2 to S2' subsites.
Enzyme-substrate contacts in the hydrolysis of ester substrates by the cysteine protease papain were investigated by systematically altering backbone hydrogen-bonding and side-chain hydrophobicExpand
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Charge is the major discriminating factor for glutathione reductase versus trypanothione reductase inhibitors.
Benson et al. (Biochem. J. 1992, 286, 9) reported three novel competitive inhibitors of trypanothione reductase (TR), which were selected to complement a hydrophobic region identified on the TRExpand
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Site‐directed mutants designed to test back‐door hypotheses of acetylcholinesterase function
The location of the active site of the rapid enzyme, acetylcholinesterase, near the bottom of a deep and narrow gorge indicates that alternative routes may exist for traffic of substrate, products orExpand
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