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Multiple binding modes for the receptor-bound conformations of cyclic AII agonists.
TLDR
Analysis of the conformational constraints imposed in these active analogs suggests that AII agonists bind to their receptor with different backbone conformations in the region of the central tyrosine residue.
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Conformational analysis of two cyclic analogs of angiotensin: implications for the biologically active conformation.
TLDR
These conformers of cyclo[Sar1, Cys3, Mpt5]-AT contain "an open turn" in the backbone of the Tyr4-Val5 residues, instead of the earlier proposed beta-like reversal, thus confirming the suggestion that the conformation(s) ensuring binding of AT analogs with specific receptors should not be described in terms of a unique backbone conformer.
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Evidence for receptor-bound turn conformations of bradykinin and angiotensin II
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Thin-layer chromatographic separation of the Z and E rotational isomers of alpha-N-nitroso-N-alkylamino acids.
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Synthesis of diazoketones derived from α-amino acids; problem of side reactions
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Synthesis of angiotensin II analogues by incorporating beta-homotyrosine or beta-homoisoleucine residues.
TLDR
The results indicate that an increase in the chain length by one carbon atom in position 4 or 5 of angiotensin II increased resistance to degradation by chymotrypsin without any increase in in vivo duration of action.
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Synthesis of Enantiomerically Pure Forms of trans‐3‐Phenylglycidic Acid.
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Synthesis of enantiomerically pure forms of trans-3-phenylglycidic acid
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[Evaluation of the presence of polychlorinated insecticides (pesticides) in trophoblasts from spontaneous and artificial abortions].
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Peptidyl diazomethylketones as cysteine protease inhibitors structurally based upon the inhibitory centers of cystatins
Six new putative cysteine protease inhibitors based upon sequences of the N-terminal binding fragments of rat cystatin A, bovine cystatin C and human cystatins D and S were synthesized, inhibitory…
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