Results 231 to 240 of about 20,368 (260)

The identification of thymidylate synthase peptide domains located in the interface region that bind thymidylate synthase mRNA

Biochemical and Biophysical Research Communications, 2002
Thymidylate synthase (TS) is a critical chemotherapeutic target and intracellular levels of TS are an important determinant of sensitivity to TS inhibitors. Translational autoregulation represents one cellular mechanism for controlling the level of expression of TS. This mechanism involves the binding of TS protein to its own messenger RNA (mRNA), thus,
Donna M, Voeller, Maria, Zajac-Kaye, Robert J, Fisher, Carmen J, Allegra   +3 more
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Insect venom peptides as potent inhibitors of Escherichia coli ATP synthase

International Journal of Biological Macromolecules, 2020
Insect venom peptides (IVPs) eumenitin, lasiocepsin, lycosin1, mastoparanB, panurgine1, and protonectin possess antibacterial properties, and the ubiquitous enzyme ATP synthase has a peptide-binding site. In the present study, we studied the effect of IVPs on binding and inhibition of three Escherichia coli strains (wild type, mutant, and null) and ...
Amon, Amini, Samah, Raheem, Amanda, Steiner, Farah, Deeba, Zulfiqar, Ahmad   +4 more
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Internalization and Stability of a Thymidylate Synthase Peptide Inhibitor in Ovarian Cancer Cells

Journal of Medicinal Chemistry, 2014
Information on the cellular internalization and stability of the ovarian cancer cell growth inhibitor peptide, LSCQLYQR (LR), is vital for lead optimization. Ad-hoc-synthesized LR/fluorescent-probe conjugates were used to monitor the internalization of the peptide.
CANNAZZA, Giuseppe, CAZZATO, ADDOLORATA STEFANIA, MARRACCINI, CHIARA, PAVESI, Giorgia, PIRONDI, SILVIA, R. Guerrini, M. Pelà, FRASSINETI, Chiara, FERRARI, Stefania, MARVERTI, Gaetano, PONTERINI, Glauco, COSTI, Maria Paola   +11 more
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A connection between antimicrobial properties of venom peptides and microbial ATP synthase

International Journal of Biological Macromolecules, 2018
Venom peptides anoplin, cupiennin 1a, latarcin 1, latarcin 3a, latarcin 5, melittin, and pandinin 2 are known to have antibacterial properties. In the current study, we examined whether the antimicrobial properties of these venom peptides have any connection to the binding and inhibition of bacterial ATP synthase.
Hiba Syed, Mohammad Tauseef, Zulfiqar Ahmad   +2 more
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Venom peptides as selective inhibitors of bacterial ATP synthase

The FASEB Journal, 2020
Background It is predicted that by the year 2050 world will face 10 million additional deaths per year due to antibiotic resistance. Misuse and overuse of antibiotics, is making microbes resistant to normally effective antibiotics.
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Use of a Synthetic Peptide as a Selective Substrate for Glycogen Synthase Kinase 3

Analytical Biochemistry, 1994
Glycogen synthase kinase 3 (GSK-3) is involved in the regulation of several metabolic enzymes and transcription factors in response to extracellular signals. Here we report the use of a synthetic peptide derived from the sequence of the cyclic AMP responsive element binding protein (CREB) as a specific substrate for GSK-3 isoforms.
Q M, Wang, P J, Roach, C J, Fiol
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A Novel Peptide Inhibits Induction of Nitric Oxide Synthase

1996
Alpha-melanocyte stimulating hormone has been shown to prevent endotoxin shock. A heptapeptide analog (HPA) has recently been synthesized and shown to be an even more potent protective agent. Since the hypotensive and toxic actions of endotoxin lipopolysaccharide (LPS) appear to involve the induction of nitric oxide synthase, we have examined the ...
G. Abou-Mohamed, A. Papapetropoulos, R. W. Caldwell   +2 more
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Ketonization of Proline Residues in the Peptide Chains of Actinomycins by a 4‐Oxoproline Synthase

ChemBioChem, 2018
AbstractX‐type actinomycins (Acms) contain 4‐hydroxyproline (Acm X0) or 4‐oxoproline (Acm X2) in their β‐pentapeptide lactone rings, whereas their α ring contains proline. We demonstrate that these Acms are formed through asymmetric condensation of Acm half molecules (Acm halves) containing proline with 4‐hydroxyproline‐ or 4‐oxoproline‐containing Acm ...
Siamak Semsary, Ivana Crnovčić, Ronja Driller, Joachim Vater, Bernhard Loll, Ullrich Keller   +5 more
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Cyclodipeptide synthases are a family of tRNA-dependent peptide bond–forming enzymes

Nature Chemical Biology, 2009
Cyclodipeptides and their derivatives belong to the diketopiperazine (DKP) family, which is comprised of a broad array of natural products that exhibit useful biological properties. In the few known DKP biosynthetic pathways, nonribosomal peptide synthetases (NRPSs) are involved in the synthesis of cyclodipeptides that constitute the DKP scaffold ...
Gondry, Muriel, Sauguet, Ludovic, Belin, Pascal, Thai, Robert, Amouroux, Rachel, Tellier, Carine, Tuphile, Karine, Jacquet, Mickaël, Braud, Sandrine, Courçon, Marie, Masson, Cédric, Dubois, Steven, Lautru, Sylvie, Lecoq, Alain, Hashimoto, Shin-Ichi, Genet, Roger, Pernodet, Jean-Luc   +16 more
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Inhibition of nitric oxide synthase with calmodulin binding peptides

2005
The constitutive isoforms of nitric oxide synthase (nNOS and eNOS) are regulated by calmodulin, which adopts an active conformation upon binding calcium and binds to target proteins. The inducible isoform of NOS (iNOS) copurifies with calmodulin [1] and was reported not to require calcium for activation [2].
Karen S. Gregson, Michael A. Marletta, Henry I. Mosberg   +2 more
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