The Relation of Neutron Dose to Chromosome Changes and Point Mutations in Drosophila. I. Translocations

1954 ◽  
Vol 88 (843) ◽  
pp. 437-459 ◽  
Author(s):  
H. J. Muller
Keyword(s):  
Point Mutations ◽  
Neutron Dose

A Novel Mutation Glyl672→Arg in Type 2A and a Homozygous Mutation in Type 2B von Willebrand Disease

1996 ◽  
Vol 76 (02) ◽  
pp. 253-257 ◽  
Author(s):  
Takeshi Hagiwara ◽  
Hiroshi Inaba ◽  
Shinichi Yoshida ◽  
Keiko Nagaizumi ◽  
Morio Arai ◽  
...  
Keyword(s):  
Missense Mutation ◽  
Novel Mutation ◽  
Point Mutations ◽  
Japanese Patients ◽  
Von Willebrand Disease ◽  
Homozygous Mutation ◽  
Missense Mutations ◽  
Reaction Products ◽  
Type 3 ◽  
Von Willebrand

SummaryGenetic materials from 16 unrelated Japanese patients with von Willebrand disease (vWD) were analyzed for mutations. Exon 28 of the von Willebrand factor (vWF) gene, where point mutations have been found most frequent, was screened by various restriction-enzyme analyses. Six patients were observed to have abnormal restriction patterns. By sequence analyses of the polymerase chain-reaction products, we identified a homozygous R1308C missense mutation in a patient with type 2B vWD; R1597W, R1597Q, G1609R and G1672R missense mutations in five patients with type 2A; and a G1659ter nonsense mutation in a patient with type 3 vWD. The G1672R was a novel missense mutation of the carboxyl-terminal end of the A2 domain. In addition, we detected an A/C polymorphism at nucleotide 4915 with HaeIII. There was no particular linkage disequilibrium of the A/C polymorphism, either with the G/A polymorphism at nucleotide 4391 detected with Hphl or with the C/T at 4891 detected with BstEll.

PREVALENCE OF COMMON MITOCHONDRIAL POINT MUTATIONS IN AUTISM

2006 ◽  
Vol 37 (S 1) ◽  
Author(s):  
FJ Serajee ◽  
H Zhong ◽  
AHMM Huq
Keyword(s):  
Point Mutations

Neutron dose evaluation of Elekta Linac at two energies (10 & 18 MV) by MCNP code and comparison with experimental measurements

2014 ◽  
Vol 6 (1) ◽  
pp. 1006-1015
Author(s):  
Negin Shagholi ◽  
Hassan Ali ◽  
Mahdi Sadeghi ◽  
Arjang Shahvar ◽  
Hoda Darestani ◽  
...  
Keyword(s):  
Monte Carlo ◽  
Measurement Data ◽  
Calculated Data ◽  
High Energy ◽  
Neutron Dose ◽  
Dose Assessment ◽  
Photon Flux ◽  
Dose Equivalent ◽  
Monte Carlo Techniques ◽  
Neutron Dose Equivalent

Medical linear accelerators, besides the clinically high energy electron and photon beams, produce other secondary particles such as neutrons which escalate the delivered dose. In this study the neutron dose at 10 and 18MV Elekta linac was obtained by using TLD600 and TLD700 as well as Monte Carlo simulation. For neutron dose assessment in 2020 cm2 field, TLDs were calibrated at first. Gamma calibration was performed with 10 and 18 MV linac and neutron calibration was done with 241Am-Be neutron source. For simulation, MCNPX code was used then calculated neutron dose equivalent was compared with measurement data. Neutron dose equivalent at 18 MV was measured by using TLDs on the phantom surface and depths of 1, 2, 3.3, 4, 5 and 6 cm. Neutron dose at depths of less than 3.3cm was zero and maximized at the depth of 4 cm (44.39 mSvGy-1), whereas calculation resulted  in the maximum of 2.32 mSvGy-1 at the same depth. Neutron dose at 10 MV was measured by using TLDs on the phantom surface and depths of 1, 2, 2.5, 3.3, 4 and 5 cm. No photoneutron dose was observed at depths of less than 3.3cm and the maximum was at 4cm equal to 5.44mSvGy-1, however, the calculated data showed the maximum of 0.077mSvGy-1 at the same depth. The comparison between measured photo neutron dose and calculated data along the beam axis in different depths, shows that the measurement data were much more than the calculated data, so it seems that TLD600 and TLD700 pairs are not suitable dosimeters for neutron dosimetry in linac central axis due to high photon flux, whereas MCNPX Monte Carlo techniques still remain a valuable tool for photonuclear dose studies.

Cupin Variants as Macromolecular Ligand Library for Stereoselective Michael Addition of Nitroalkanes

2019 ◽  
Author(s):  
Nobutaka Fujieda ◽  
Miho Yuasa ◽  
Yosuke Nishikawa ◽  
Genji Kurisu ◽  
Shinobu Itoh ◽  
...  
Keyword(s):  
Michael Addition ◽  
In Silico ◽  
Addition Reaction ◽  
Single Point ◽  
Point Mutations ◽  
Unsaturated Ketone ◽  
Michael Addition Reaction ◽  
Beta Barrel ◽  
Cupin Superfamily ◽  
Single Point Mutations

Cupin superfamily proteins (TM1459) work as a macromolecular ligand framework with a double-stranded beta-barrel structure ligating to a Cu ion through histidine side chains. Variegating the first coordination sphere of TM1459 revealed that H52A and H54A/H58A mutants effectively catalyzed the diastereo- and enantio-selective Michael addition reaction of nitroalkanes to an α,β-unsaturated ketone. Moreover, in silico substrate docking signified C106N and F104W single-point mutations, which inverted the diastereoselectivity of H52A and further improved the stereoselectivity of H54A/H58A, respectively.

The Impact of Bioconjugation on the Interfacial Activity of a Protein Biosurfactant

2018 ◽  
Author(s):  
Hossam H Tayeb ◽  
Marina Stienecker ◽  
Anton Middelberg ◽  
Frank Sainsbury
Keyword(s):  
Polyethylene Glycol ◽  
Colloidal Stability ◽  
Point Mutations ◽  
Pharmaceutical Formulations ◽  
Industrial Processes ◽  
Parent Molecule ◽  
Site Specific ◽  
Interfacial Activity ◽  
Surface Active ◽  
The Impact

Biosurfactants, are surface active molecules that can be produced by renewable, industrially scalable biologic processes. DAMP4, a designer biosurfactant, enables the modification of interfaces via genetic or chemical fusion to functional moieties. However, bioconjugation of addressable amines introduces heterogeneity that limits the precision of functionalization as well as the resolution of interfacial characterization. Here we designed DAMP4 variants with cysteine point mutations to allow for site-specific bioconjugation. The DAMP4 variants were shown to retain the structural stability and interfacial activity characteristic of the parent molecule, while permitting efficient and specific conjugation of polyethylene glycol (PEG). PEGylation results in a considerable reduction on the interfacial activity of both single and double mutants. Comparison of conjugates with one or two conjugation sites shows that both the number of conjugates as well as the mass of conjugated material impacts the interfacial activity of DAMP4. As a result, the ability of DAMP4 variants with multiple PEG conjugates to impart colloidal stability on peptide-stabilized emulsions is reduced. We suggest that this is due to constraints on the structure of amphiphilic helices at the interface. Specific and efficient bioconjugation permits the exploration and investigation of the interfacial properties of designer protein biosurfactants with molecular precision. Our findings should therefore inform the design and modification of biosurfactants for their increasing use in industrial processes, and nutritional and pharmaceutical formulations.

Coaction of Electrostatic and Hydrophobic Interactions: Dynamic Constraints on Disordered TrkA Juxtamembrane Domain

2019 ◽  
Author(s):  
Zichen Wang ◽  
Huaxun Fan ◽  
Xiao Hu ◽  
John Khamo ◽  
Jiajie Diao ◽  
...  
Keyword(s):  
Single Molecule ◽  
Protein Function ◽  
Hydrophobic Interactions ◽  
Transmembrane Helix ◽  
Point Mutations ◽  
Salt Bridge ◽  
Receptor Activation ◽  
Membrane Dynamics ◽  
Juxtamembrane Domain ◽  
Joint Work

<p>The receptor tyrosine kinase family transmits signals into cell via a single transmembrane helix and a flexible juxtamembrane domain (JMD). Membrane dynamics makes it challenging to study the structural mechanism of receptor activation experimentally. In this study, we employ all-atom molecular dynamics with Highly Mobile Membrane-Mimetic to capture membrane interactions with the JMD of tropomyosin receptor kinase A (TrkA). We find that PIP<sub>2 </sub>lipids engage in lasting binding to multiple basic residues and compete with salt bridge within the peptide. We discover three residues insertion into the membrane, and perturb it through computationally designed point mutations. Single-molecule experiments indicate the contribution from hydrophobic insertion is comparable to electrostatic binding, and in-cell experiments show that enhanced TrkA-JMD insertion promotes receptor ubiquitination. Our joint work points to a scenario where basic and hydrophobic residues on disordered domains interact with lipid headgroups and tails, respectively, to restrain flexibility and potentially modulate protein function.</p>

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