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1,084 results for “substrate”
Fig. 5 in 21-Hydroxypregnane 21-O-malonylation, a crucial step in cardenolide biosynthesis, can be achieved by substrate-promiscuous BAHD-type phenolic glucoside malonyltransferases from Arabidopsis thaliana and homolog proteins from Digitalis lanata
Fig. 5. Expression of Dlmat1, Dlmat2, Dlmat3, and Dlmat4 in different plant tissues measured by real-time quantitative PCR (qPCR). Expression rates are standardized to the values of the actin transcript in each tissue and were displayed in relation to the expression in young leaves (set to equal 1) for each Dlmat gene.
Fig. 1 in A single residue determines substrate preference in benzylisoquinoline alkaloid N-methyltransferases
Fig. 1. Involvement of N-methyltransferases in BIA biosynthesis. Coclaurine N-methyltransferase (CNMT) acts in the core BIA pathway and converts an unmethylated secondary amine to a mono-methylated tertiary amine. Reticuline N-methyltransferase (RNMT) and Pavine N-methyltransferase (PavNMT) act in several branch pathways and primarily convert mono-methylated tertiary amines into a di-methylated quaternary amines. Tetrahydroprotoberberine N-methyltransferase (TNMT) acts in other branch pathways and converts a bicyclic unmethylated tertiary amine into a quaternary amine. † denotes activities that have been demonstrated in vitro but not conclusively associated with the enzyme via in planta experimental evidence (e.g. gene silencing).
Fig. 5 in A single residue determines substrate preference in benzylisoquinoline alkaloid N-methyltransferases
Fig. 5. Sequence-based prediction and in vivo screening of putative CNMT and RNMT enzymes. (A) The identity of residue 204 (E, glutamic acid; G, glycine) was used to predict CNMT- or RNMT-like function, respectively. (B) Overall amino acid sequence identity does not distinguish CNMT- or RNMT-like enzymes from each other (Supplementary Dataset 5). (C) Formation of N-methylated products following supplementation of yeast cultures with (S)-coclaurine (white bars), (S)-N- methylcoclaurine (black bars) and (S)-reticuline (grey bars). For each substrate, the culture with the greatest mean product concentration normalized to optical density was set to 100% and all other values were scaled accordingly (30.7μM OD−1 (S)-N-methylcoclaurine, HCANMT1; 3.4μM OD−1 (S)-N,N-dimethylcoclaurine, SCANMT1; 2.0μM OD−1 (S)-tembetarine, SCANMT1). Error bars represent standard deviation of four replicate cultures. Western blot analysis of NMT expression is show in Supplementary Fig. 6.
Fig. 3 in A single residue determines substrate preference in benzylisoquinoline alkaloid N-methyltransferases
Fig. 3. Enzymatic activities of wild-type CNMT, wild-type RNMT and reciprocal 204 mutants. (A) Activity with canonical CNMT substrate (S)-coclaurine. Black bars indicate mono-methylated product (S)-N-methylcoclaurine and grey bars indicate di-methylated product (S)-N,N-dimethylcoclaurine. (B) Activity with tertiary amine substrate (S)-N-methylcoclaurine. (C) Activity with canonical RNMT substrate (S)-reticuline. Products were identified and quantified by LC-MS/MS. Error bars represent standard deviation of three replicates. WT denotes results corresponding to the wild-type enzyme.
Fig. 2 in A single residue determines substrate preference in benzylisoquinoline alkaloid N-methyltransferases
Fig. 2. Analysis of key active site residues in BIA N-methyltransferases. (A) Primary sequence alignment of functionally validated BIA NMTs showing that residue 204 is conserved within BIA NMT subtypes (i.e. E in CNMTs and TNMTs, G in RNMTs, A in PavNMTs) whereas residues previously suggested to form a catalytic dyad (E207 and H208) are universally conserved. (B, C) Docking of RNMT substrate (S)-reticuline (cyan) into the active site of (B) CjCNMT (PDB 6GKV) and (C) PsRNMT (homology model) reveals a steric clash between the N-methyl group and residue E204 but not G204. S-Adenosylhomocysteine is shown in pink. Spheres represent Van der Waals radii and the distance between key atoms is given in angstroms.
Fig. 4 in A single residue determines substrate preference in benzylisoquinoline alkaloid N-methyltransferases
Fig. 4. Superimposition of residue 204 identity on a maximum-likelihood phylogenetic analysis of N-methyltransferase gene candidates. The cladogram was adapted from that deposited in DRYAD by Hagel et al. (2015b) (https://doi.org/10.5061/dryad.bh276/18) and the corresponding sequences are described in Supplementary Dataset 4. CjCNMT was not included in the original analysis but is most similar to TfCNMT (86% amino acid identity). Key nodes are labelled with support values representing the number of 1000 bootstrapped trees in which the associated taxa clustered together. Putative BIA NMT sequences were aligned by Clustal Omega and the identity of the residue corresponding to E204 in CjCNMT was mapped onto each taxa (glutamic acid, green; glycine, purple; alanine, cyan; glutamine, yellow; serine; orange). BIA NMTs for which in vitro functional characterization data was available are indicated with black arrows and those subjected to yeast-based in vivo characterization in this work are indicated with white arrows. Prior to this report, sequence-based prediction of BIA NMT sub-functionalization was reliable for TNMT-like enzymes only due to their clustering as a single well-defined clade. CNMT-, RNMT- and PavNMT-like sequences are distributed amongst several less well-defined clades.
Role of a capping layer on the crystalline structure of Sn thin films grown at cryogenic temperatures on InSb substrates
<p>These are the supplementary data supporting the main publication.</p>
Data and code for paper "Stealth echolocation in aerial hawking bats reflects a substrate gleaning ancestry"
<p>- Bat_gleaning_ancestral_recon.R (in folder "AncestralStateReconstruction") reads shi_rabosky_2015_spp1A.csv and does the ancestral state reconstruction</p> <p>- Lewanzik.et.al_Lombard.effect.R (in folder "LombardEffect") reads Lewanzik.et.al_Lombard.data.csv to produce Fig. 2 and to model source levels as a function of noise treatment (silence vs white noise playback)</p> <p>- figure3.m and figure4.m (in folder "EcholocationParameters") is the Matlab code to produce Fig. 3 and Fig. 4, respectively. These .m-files use code in the "private" folder and data (.mat files) in the "Barbastella" and "Pygmaeus" folders.</p>
The Structural Role of N170 in Substrate-assisted Deacylation in KPC-2 β-Lactamase
<p>The dataset contains trajectories, structure files, HILLS files and COLVAR files for D179 WT, D179A, D179Q, D179N, D179Y, R164 WT, R164S, R164H</p>
DEEP Substrate Mapping Versus Activation Mapping for VT
ClinicalTrials.gov study NCT06371729. IPD Sharing: NO. Countries: 1. Publications: 3.
A Pharmacokinetic Study to Evaluate the Drug Interaction Between SHR0302 and CYP Substrates in Healthy Volunteers
ClinicalTrials.gov study NCT05392127. IPD Sharing: UNDECIDED. Countries: 1. Publications: 1.
Neural Substrates Underlying Adaptations in Manual Dexterity of Older Adults
ClinicalTrials.gov study NCT07011160. IPD Sharing: NO. Countries: 1. Publications: 3.
Psycho-biological Substrates of Therapeutic Benefit of Thermal Cure on Generalized Anxiety Disorders
ClinicalTrials.gov study NCT03277339. IPD Sharing: Not stated. Countries: 1. Publications: 5.
SMS: Substrate Modification Study in Patients Getting an Implantable Cardioverter Defibrillator (ICD)
ClinicalTrials.gov study NCT00170287. IPD Sharing: NO. Countries: 2. Publications: 1.
Substrate and Trigger Ablation for Reduction of Atrial Fibrillation Trial - Star AF II Study
ClinicalTrials.gov study NCT01203748. IPD Sharing: Not stated. Countries: 2. Publications: 3.
Trigger- vs. Substrate-Ablation for Paroxysmal Atrial Fibrillation
ClinicalTrials.gov study NCT00196183. IPD Sharing: Not stated. Countries: 1. Publications: 2.
A Drug-drug Interaction Study Between GLPG1205 and a Cocktail of CYP450 Substrates in Healthy Male Subjects
ClinicalTrials.gov study NCT02623296. IPD Sharing: Not stated. Countries: 1. Publications: 1.
IL-6 Regulation of Substrate Metabolism and Influence of Obesity
ClinicalTrials.gov study NCT03967691. IPD Sharing: NO. Countries: 1. Publications: 2.
Trial to Evaluate the Efficacy and Safety of Substrate Ablation of Monomorphic Ventricular Tachycardia
ClinicalTrials.gov study NCT03734562. IPD Sharing: UNDECIDED. Countries: 1. Publications: 2.
a Novel Individualized Substrate Modification Approach for the Treatment of Long-standing Persistent Atrial Fibrillation
ClinicalTrials.gov study NCT02477592. IPD Sharing: Not stated. Countries: 1. Publications: 12.
ScienceDex guides
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These curated guides explain access requirements, typical timelines, costs, and reuse considerations for widely used research datasets.
Allen Brain Atlas
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DANDI Archive for NWB datasets
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International Brain Laboratory public data
The International Brain Laboratory public data releases expose standardized mouse decision-making experiments, including Neuropixels recordings, widefield calcium imaging, behavior, and session metadata accessed through the ONE API.
OpenNeuro
OpenNeuro is a free, open platform for sharing neuroimaging datasets, with public search, dataset pages, and download paths for web, S3, DataLad, and the OpenNeuro CLI.