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71.
Liane FM Finotelo Paulo JS Amaral Julio C Pieczarka Edivaldo HC de Oliveira Alcides Pissinati Michaela Neusser Stephan Müller Cleusa Y Nagamachi 《BMC evolutionary biology》2010,10(1):189
Background
The New World monkey (Platyrrhini) subfamily Pitheciinae is represented by the genera Pithecia, Chiropotes and Cacajao. In this work we studied the karyotypes of Pithecia irrorata (2n = 48) and Cacajao calvus rubicundus (2n = 45 in males and 2n = 46 in females) by G- and C-banding, NOR staining and chromosome painting using human and Saguinus oedipus whole chromosome probes. The karyotypes of both species were compared with each other and with Chiropotes utahicki (2n = 54) from the literature. 相似文献72.
Benjamin P. Isaacoff Yilai Li Stephen A. Lee Julie S. Biteen 《Biophysical journal》2019,116(6):975-982
Single-molecule and super-resolution imaging relies on successful, sensitive, and accurate detection of the emission from fluorescent molecules. Yet, despite the widespread adoption of super-resolution microscopies, single-molecule data processing algorithms can fail to provide accurate measurements of the brightness and position of molecules in the presence of backgrounds that fluctuate significantly over time and space. Thus, samples or experiments that include obscuring backgrounds can severely, or even completely, hinder this process. To date, no general data analysis approach to this problem has been introduced that is capable of removing obscuring backgrounds for a wide variety of experimental modalities. To address this need, we present the Single-Molecule Accurate LocaLization by LocAl Background Subtraction (SMALL-LABS) algorithm, which can be incorporated into existing single-molecule and super-resolution analysis packages to accurately locate and measure the intensity of single molecules, regardless of the shape or brightness of the background. Accurate background subtraction is enabled by separating the foreground from the background based on differences in the temporal variations of the foreground and the background (i.e., fluorophore blinking, bleaching, or moving). We detail the function of SMALL-LABS here, and we validate the SMALL-LABS algorithm on simulated data as well as real data from single-molecule imaging in living cells. 相似文献
73.
Shechinah Felice Choragudi Ganesh Kumar Veeramachaneni BV Raman Bondili JS 《Bioinformation》2014,10(8):507-511
Endo- β-N-acetylgucosaminidases (ENGases) are the enzymes that catalyze both hydrolysis and
transglycosylation reactions. It is of interest to study ENGases because of their ability to synthesize glycopeptides.
Homology models of Human, Arabidopsis thaliana and Sorghum ENGases were developed and their active sites
marked based on information available from Arthrobacter protophormiae (PDB ID: 3FHQ) ENGase. Further, these
models were docked with the natural substrate GlcNAc-Asn and the inhibitor Man3GlcNAc-thiazoline. The catalytic
triad of Asn, Glu and Tyr (N171, E173 and Y205 of bacteria) were found to be conserved across the phyla. The crucial
Y299F mutation showing 3 times higher transglycosylation activity than in wild type Endo-A is known. The hydrolytic
activity remained unchanged in bacteria, while the transglycosylation activity increased. This Y to F change is found
to be naturally evolved and should be attributing higher transglycosylation rates in human and Arabidopsis thaliana
ENGases. Ligand interactions Ligplots revealed the interaction of amino acids with hydrophobic side chains and polar
uncharged side chain amino acids. Thus, structure based molecular model-ligand interactions provide insights into
the catalytic mechanism of ENGases and assist in the rational engineering of ENGases. 相似文献
74.