4.6.1.18 (-)-epigallocatechin-3-gallate noncompetitive 2518 4.6.1.18 1-(2,5-dideoxy-5-(4-carboxypiperidinyl)-beta-D-threo-pentofuranosyl)thymine - 86283 4.6.1.18 1-(2,5-dideoxy-5-pyrrolidin-1-yl-beta-L-erythro-pentofuranosyl)-5-methylpyrimidine-2,4(1H,3H)-dione - 80320 4.6.1.18 1-(5-deoxy-5-morpholin-4-yl-alpha-L-arabinofuranosyl)pyrimidine-2,4(1H,3H)-dione - 80316 4.6.1.18 1-(5-deoxy-5-piperidin-1-yl-alpha-L-arabinofuranosyl)pyrimidine-2,4(1H,3H)-dione - 80317 4.6.1.18 1-(5-deoxy-5-pyrrolidin-1-yl-alpha-L-arabinofuranosyl)pyrimidine-2,4(1H,3H)-dione - 80318 4.6.1.18 1-(5-deoxy-5-[4-(ethoxycarbonyl)piperidin-1-yl]-alpha-L-arabinofuranosyl)pyrimidine-2,4(1H,3H)-dione - 80315 4.6.1.18 2'(3')Nucleotides - 98592 4.6.1.18 2',3'-dideoxy-3'-(gamma-aminobutyric acid)amino thymidine - 159628 4.6.1.18 2',3'-dideoxy-3'-D-leucylamino thymidine - 159625 4.6.1.18 2',3'-dideoxy-3'-glycylamino thymidine - 159621 4.6.1.18 2',3'-dideoxy-3'-L-alanylamino thymidine - 159622 4.6.1.18 2',3'-dideoxy-3'-L-histidinylamino thymidine - 159626 4.6.1.18 2',3'-dideoxy-3'-L-leucylamino thymidine - 159624 4.6.1.18 2',3'-dideoxy-3'-L-serinylamino thymidine occupies the active site of ribonuclease A and preferential perturbs the pKa value of His-119 by its free amino group as found from 1H NMR studies, compounds with polar amino acid side chains such as Ser-aT, Tyr-aT and Trp-aT (except His-aT) are more efficient inhibitors compared to those having hydrophobic side chains 80321 4.6.1.18 2',3'-dideoxy-3'-L-tryptophanylamino thymidine compounds with polar amino acid side chains such as Ser-aT, Tyr-aT and Trp-aT (except His-aT) are more efficient inhibitors compared to those having hydrophobic side chains 159627 4.6.1.18 2',3'-dideoxy-3'-L-tyrosylamino thymidine compounds with polar amino acid side chains such as Ser-aT, Tyr-aT and Trp-aT (except His-aT) are more efficient inhibitors compared to those having hydrophobic side chains 80322 4.6.1.18 2',3'-dideoxy-3'-L-valinylamino thymidine - 159623 4.6.1.18 2'-Deoxynucleotides - 98378 4.6.1.18 3'-CMP strong binding by the wild-type enzyme, reduced binding by enzyme mutants T17A and T82A, kinetics, overview 2000 4.6.1.18 3'-CMP natural product inhibitor, NMR binding analysis, overview 2000 4.6.1.18 3'-deoxy-3'-[4-(ethoxycarbonyl)piperidin-1-yl] uridine - 58872 4.6.1.18 3'-deoxy-3'-[4-carboxypiperidin-1-yl] uridine - 58873 4.6.1.18 3'-TMP a competitive inhibitor analogue of the 3'-CMP and 3'-UMP natural product inhibitors, the enzyme shows very high affinty and strong binding with 3'-TMP. Binding of 3'-TMP is very similar to other natural and nonnatural pyrimidine ligands, so single nucleotide affinity is independent of the presence or absence of a 2'-hydroxyl on the ribose moiety of pyrimidines 10494 4.6.1.18 3'-UMP natural product inhibitor, NMR binding analysis, overview 2312 4.6.1.18 3-amino-N-[2-hydroxymethyl-5-(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-tetrahydro-furan-3-yl]-succinamic acid - 86287 4.6.1.18 3-N-piperidine-4-carboxyl-3-deoxy-ara-uridine binding of two inhibitor molecules in the central cavity of enzyme 138765 4.6.1.18 4-[2-hydroxymethyl-5-(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-tetrahydro-furan-3-ylcarbamoyl]-butyric acid - 159620 4.6.1.18 5'-AMP - 236 4.6.1.18 5'-carboxyadenosine - 86285 4.6.1.18 5'-carboxythymidine - 86286 4.6.1.18 5'-deoxy-5'-N-(4-carboxypiperidinyl)thymidine - 86282 4.6.1.18 5'-deoxy-5'-N-(4-carboxypiperidinyl)uridine - 86281 4.6.1.18 5'-deoxy-5'-piperidin-1-ylthymidine - 80319 4.6.1.18 5'-GMP - 1022 4.6.1.18 5'-N-(4-carboxypiperidinyl)-2',3'-didehydro-3',5'-dideoxythymidine - 86284 4.6.1.18 5'-phospho-2'-deoxyuridine-3-diphosphate (P-5)-adenosine-3'-phosphate i.e. pdUppA-3'-p, multi-ns molecular dynamics simulations of enzyme in complex with inhibitor 138766 4.6.1.18 5-aminoethyluracil - 102298 4.6.1.18 5-Nitrouracil - 4494 4.6.1.18 adenosine 5'-phosphate - 4780 4.6.1.18 arsenite - 397 4.6.1.18 ATP 5’-ATP binds with the adenine occupying the B2 subsite in the manner of an RNA substrate but with the gamma-phosphate at the P1 subsite, crystal structure of the complex with pancreatic ribonuclease A 4 4.6.1.18 aurintricarboxylic acid alters the three-dimensional conformation, dissociation constant of ribonuclease A with aurintricarboxylic acid is 2.33 microM 1818 4.6.1.18 BeCl2 - 102506 4.6.1.18 CaCl2 - 218 4.6.1.18 chitosan molecular weight about 6 kDA, complex formation with enzyme due to establishment of 5-6 ion pairs 1123 4.6.1.18 chloride - 298 4.6.1.18 Copolymer of glutamic acid and tyrosine - 99026 4.6.1.18 CuSO4 - 263 4.6.1.18 cytidine - 372 4.6.1.18 cytidine 2',3'-cyclic monophosphate substrate inhibition of PE5 mutant enzyme variants at higher substrate concentration 161097 4.6.1.18 cytidine-N3-oxide 2'-phosphate - 101869 4.6.1.18 cytosolic ribonuclease inhibitor with CpA as substrate, both isoenzymes are fully susceptible to inhibition 34599 4.6.1.18 cytosolic ribonuclease inhibitor protects cells against exogenous ribonucleases, variants of pancreatic ribonuclease that evade ribonuclease inhibitor are cytotoxic, molecular evolution of ribonuclease inhibitor suggests to be a means to enhance the cytotoxicity of mammalian ribonucleases 34599 4.6.1.18 cytosolic ribonuclease inhibitor RI, from Sus scrofa, binding of the RI molecule to the N-terminal RNase A entity, analysis of crystal structures of the RI–RNase A complex and the SGRSGRSG-RNase A tandem enzyme, PDB-ID 1DFJ, overview 34599 4.6.1.18 cytosolic RNase inhibitor - 197066 4.6.1.18 diethylpyrocarbonate among the His residues of RNase A, His48 is not accessible to react with diethylpyrocarbonate 2270 4.6.1.18 epicatechin 0.04 mM, 4.4% inhibition, noncompetitve, CD spectral analysis of complex with enzyme, preferred site of binding is around residues 34-39 with possible hydrogen bonding to K7 and R10 1161 4.6.1.18 epicatechin gallate 0.04 mM, 12.7% inhibition, noncompetitve, CD spectral analysis of complex with enzyme, preferred site of binding is around residues 34-39 with possible hydrogen bonding to K7 and R10 3466 4.6.1.18 epigallocatechin 0.04 mM, 6.9% inhibition, noncompetitve, CD spectral analysis of complex with enzyme, preferred site of binding is around residues 34-39 with possible hydrogen bonding to K7 and R10 2229 4.6.1.18 epigallocatechin gallate 0.04 mM, 18.4% inhibition, noncompetitve, CD spectral analysis of complex with enzyme, preferred site of binding is around residues 34-39 with possible hydrogen bonding to K7 and R10 1234 4.6.1.18 FeSO4 - 655 4.6.1.18 folic acid inhibitor when 2',3'-CMP is substrate not when RNA is substrate 2840 4.6.1.18 green tea catechins noncompetitive 58871 4.6.1.18 H2O2 - 22 4.6.1.18 HP-RNase antibodies affinity purified polyclonal antibodies against human pancreatic RNase. 94% inhibition with 50 ng 123058 4.6.1.18 Hydrobenzoinphosphate - 93647 4.6.1.18 inhibit-Ace 86% inhibition at 6 U/ml 123057 4.6.1.18 iodoacetate - 93 4.6.1.18 liver natural inhibitor - 102964 4.6.1.18 Mercury hematoporphyrin - 98052 4.6.1.18 Mg2+ reduces activity in the presence of K+ 6 4.6.1.18 Mg2+ - 6 4.6.1.18 additional information not inhibitory: monoglucosamine up to 2 mM 2 4.6.1.18 additional information not inhibitory: Mg2+, phosphate, EDTA 2 4.6.1.18 additional information construction of enzyme dimer composed of monomeric units covalently linked by a single amide bond between the side-chains of residues K66 and E9 by incubation of a lyophilized preparation of enzyme under vacuum at 85°C. Dimer exhibits a twofold increase in activity over monomeric enzyme and is not inhibited by the cellular ribonuclease inhibitor protein 2 4.6.1.18 additional information As(III) species, by avid coordination to the cysteine residues of unfolded reduced proteins, can compromise protein folding pathways, monomethylarsenous acid catalyzes the formation of amyloid-like monodisperse fibrils using reduced ribonuclease A 2 4.6.1.18 additional information agarose gel and precipitation assays show that the spacer length and the pKa of the carboxylic group have an important role in the inhibitory capacity 2 4.6.1.18 additional information inhibitor synthesis, molecular docking to the enzyme, interaction of inhibitors with hydrogen bonding network formation between His12 and His119 of RNase A, overview 2 4.6.1.18 additional information inhibitor synthesis, kinetics, and docking, overview 2 4.6.1.18 additional information enzyme-inhibitor binding and interaction analysis, kinetics, overview 2 4.6.1.18 N-[2-hydroxymethyl-5-(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-tetrahydro-furan-3-yl]-malonamic acid - 80312 4.6.1.18 N-[2-hydroxymethyl-5-(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-tetrahydro-furan-3-yl]-oxalamic acid - 80311 4.6.1.18 N-[2-hydroxymethyl-5-(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-tetrahydro-furan-3-yl]-succinamic acid - 80313 4.6.1.18 NaCl - 42 4.6.1.18 NaCl above 0.25 M 42 4.6.1.18 NaCl 0.15 M or above 42 4.6.1.18 NADP+ crystal structure of the complex with pancreatic ribonuclease A 10 4.6.1.18 NADPH crystal structure of the complex with pancreatic ribonuclease A 5 4.6.1.18 oligo(vinylsulfonic acid) potent competitive inhibitor making nearly 8 favorable Coulombic interactions with the enzyme. Oligo(vinylsulfonic acid) is inexpensive and extremely stable. Accoringly oligo(vinylsulfonic acid) has the potential to be useful prophylactic in many chemical, biochemical, and biotechnical experiments involving RNA 35448 4.6.1.18 oligonucleotides e.g. ApUp 1834 4.6.1.18 P1,P3-bis(5'-adenosyl) triphosphate crystal structure of the complex with pancreatic ribonuclease A 5593 4.6.1.18 penicillin - 2664 4.6.1.18 Phenylphosphate - 5201 4.6.1.18 Pholiota nameko polysaccharide linear mixed-type inhibition, noncompetitive inhibition is predominant over competitive inhibition 36966 4.6.1.18 phosphate - 16 4.6.1.18 PO43- - 867 4.6.1.18 poly(vinylsulfonic acid) - 129670 4.6.1.18 poly(vinylsulfuric acid) - 129671 4.6.1.18 Polyanions natural and synthetic, free poly(A), poly(U) 21048 4.6.1.18 putrescine - 155 4.6.1.18 Pyrophosphate crystal structure of the complex with pancreatic ribonuclease A 31674 4.6.1.18 ribonuclease inhibitor cytoplasmic 3126 4.6.1.18 ribonuclease inhibitor forms a tight complex with RNase A 3126 4.6.1.18 ribonuclease inhibitor - 3126 4.6.1.18 ribonuclease inhibitor RI, 97% inhibition at 6 U/ml 3126 4.6.1.18 ribonuclease inhibitor extremely tight complex with bovine ribonuclease inhibitor, Kd value 0.69 fM. Kd value of complex with human ribonuclease inhibitor 0.34 fM 3126 4.6.1.18 ribonuclease inhibitor tight complex with human ribonuclease inhibitor, Kd value 0.34 fM. Kd value of complex with bovine ribonuclease inhibitor 35 fM 3126 4.6.1.18 ribonuclease inhibitor human placental ribonuclease inhibitor; human placental ribonuclease inhibitor 3126 4.6.1.18 ribonuclease inhibitor crystallization data of complex with enzyme, formation of 19 hydrogen bonds results in extreme stability of complex. Kd value 29 * 10-8 nM 3126 4.6.1.18 ribonuclease inhibitor human placental ribonuclease inhibitor, characterization of its tryptophan residues in the complex with the enzyme. The complex formation results in a more heterogenous environment for both of the optically resolved residues W19 and W375. W19 moves slightly toward a more hydrophobic region, ant the environment of W375 becomes less solvent exposed 3126 4.6.1.18 ribonuclease inhibitor CPRI scavenger of pancreatic-type ribonucleases, chemiluminescence assay to determine radical scavenging activities toward different reactive oxygen species (ROS) including superoxide anion, hydroxyl radical, lipid-derived radicals and singlet oxygen 138764 4.6.1.18 ribonuclease protein inhibitor the native enzyme is an equilibrium mixture of two isomers, MxM and M=M. In the former the two subunits swap their N-terminal helices. In the reducing environment of the cytosol, isoform M=M dissociates into monomers, which are strongly inhibited by ribonuclease protein inhibitor, wheras isoform MxM remains as a non-covalent dimer which evades ribonuclease protein inhibitor 129672 4.6.1.18 RNase inhibitor RNase A, like most monomeric RNases, is strongly bound and inactivated in mammalian cells by the RNase inhibitor 197067 4.6.1.18 RNasin 50 kDa protein inhibitor isolated from human placenta 66115 4.6.1.18 RNasin for investigating protein translocation in vitro, rough membrane vesicles of endoplasmic reticular origin from the pancreas of different livestock animals can be used as a valuable alternative to the dog source. Since the mRNA in the translation mixture is degraded by ribonucleases present in the membrane fraction, the membrane stocks were diluted in membrane buffer and pretreated with increasing amounts of the recombinant RNase inhibitor RNasin (Promega) 66115 4.6.1.18 Selenite - 1937 4.6.1.18 spermidine RNA-binding enzyme activity is regulated through spermidine-induced changes in the charge and structure of the RNA substrate. Spermidine transiently stabilizes RNA sub-populations by binding both specifically and nonspecifically 148 4.6.1.18 spermine at 0.13 mM: inhibition, at 0.02 M: activity towards cyclic substrates and poly(C) is activated, not towards poly(U) 197 4.6.1.18 thiocyanate inactivation due to expansion of the enzyme surface and elongation of the catalytic center 931 4.6.1.18 trichloroacetic acid partially inactivates 48176 4.6.1.18 Urea mechanism of inhibition, urea inhibits ribonuclease A competitively over a concentration range from 100 mM to 4.0 M, urea with its high dipolar moment is a competitive inhibitor and a very high concentration (more than 4.0 M) of it could denature the enzyme, beginning the interaction with the protein at the active center 116 4.6.1.18 uridine 5'-diphosphate competitive inhibitor 21718 4.6.1.18 uridine 5'-phosphate competitive inhibitor 7434 4.6.1.18 vitamin B12 - 878 4.6.1.18 VO2+ in complex with nucleotide monophosphate 10809 4.6.1.18 ZnSO4 - 485