Study of the core-corona structure formed during the explosion of an aluminum wire in vacuum

The optimized extrusion conditions from the present research were the extrusion temperature of 573~623K and the extrusion ratio(A0/A) of 21.39. Above the extrusion temperature of 623K, the fracture of sheath material was observed. It is due to the difference of flow stress between the sheath material and the core material during extrusion process. The bonding strength increased with increasing the extrusion temperature and the extrusion ratio. The bonding strength increased with increasing the annealing temperature. However, over 573K, it decreased abruptly since the thick and brittle intermetallic compounds of larger than 3µm were formed. The electricalconductivity of copper clad aluminum wire was about 70%IACS without annealing.

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Cep192, a Novel Missing Link between the Centrosomal Core and Corona in Dictyostelium Amoebae

Cells ◽

10.3390/cells10092384 ◽

2021 ◽

Vol 10 (9) ◽

pp. 2384

Author(s):

Valentin Pitzen ◽

Sophia Sander ◽

Otto Baumann ◽

Ralph Gräf ◽

Irene Meyer

Keyword(s):

Research Group ◽

Fusion Proteins ◽

Outer Core ◽

Core Structure ◽

The Core ◽

Marker Proteins ◽

Interaction Partners ◽

Core Components ◽

Corona Structure ◽

Centrosomal Proteins

The Dictyostelium centrosome is a nucleus-associated body with a diameter of approx. 500 nm. It contains no centrioles but consists of a cylindrical layered core structure surrounded by a microtubule-nucleating corona. At the onset of mitosis, the corona disassembles and the core structure duplicates through growth, splitting, and reorganization of the outer core layers. During the last decades our research group has characterized the majority of the 42 known centrosomal proteins. In this work we focus on the conserved, previously uncharacterized Cep192 protein. We use superresolution expansion microscopy (ExM) to show that Cep192 is a component of the outer core layers. Furthermore, ExM with centrosomal marker proteins nicely mirrored all ultrastructurally known centrosomal substructures. Furthermore, we improved the proximity-dependent biotin identification assay (BioID) by adapting the biotinylase BioID2 for expression in Dictyostelium and applying a knock-in strategy for the expression of BioID2-tagged centrosomal fusion proteins. Thus, we were able to identify various centrosomal Cep192 interaction partners, including CDK5RAP2, which was previously allocated to the inner corona structure, and several core components. Studies employing overexpression of GFP-Cep192 as well as depletion of endogenous Cep192 revealed that Cep192 is a key protein for the recruitment of corona components during centrosome biogenesis and is required to maintain a stable corona structure.

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Poly(Ethylene Glycol)-b-Poly(D,L-Lactide) Nanoparticles as Potential Carriers for Anticancer Drug Oxaliplatin

Molecules ◽

10.3390/molecules26030602 ◽

2021 ◽

Vol 26 (3) ◽

pp. 602

Author(s):

Yulia A. Kadina ◽

Ekaterina V. Razuvaeva ◽

Dmitry R. Streltsov ◽

Nikita G. Sedush ◽

Eleonora V. Shtykova ◽

...

Keyword(s):

Ethylene Glycol ◽

Anticancer Drug ◽

Anticancer Agent ◽

Block Length ◽

Poly Ethylene Glycol ◽

X Ray ◽

The Core ◽

X Ray Scattering ◽

Corona Structure ◽

Poly Ethylene

Nanoparticles based on biocompatible methoxy poly(ethylene glycol)-b-poly(D,L-lactide) (mPEG113-b-P(D,L)LAn) copolymers as potential vehicles for the anticancer agent oxaliplatin were prepared by a nanoprecipitation technique. It was demonstrated that an increase in the hydrophobic PLA block length from 62 to 173 monomer units leads to an increase of the size of nanoparticles from 32 to 56 nm. Small-angle X-ray scattering studies confirmed the “core-corona” structure of mPEG113-b-P(D,L)LAn nanoparticles and oxaliplatin loading. It was suggested that hydrophilic oxaliplatin is adsorbed on the core-corona interface of the nanoparticles during the nanoprecipitation process. The oxaliplatin loading content decreased from 3.8 to 1.5% wt./wt. (with initial loading of 5% wt./wt.) with increasing PLA block length. Thus, the highest loading content of the anticancer drug oxaliplatin with its encapsulation efficiency of 76% in mPEG113-b-P(D,L)LAn nanoparticles can be achieved for block copolymer with short hydrophobic block.

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What face familiarity feelings say about the lateralization of specific entities within the core system

Behavioral and Brain Sciences ◽

10.1017/s0140525x19001778 ◽

2019 ◽

Vol 42 ◽

Author(s):

Guido Gainotti

Keyword(s):

Temporal Lobe ◽

Memory System ◽

Core System ◽

The Core ◽

Memory Traces ◽

Specific Memory ◽

Target Article ◽

Temporal Structures ◽

The Right

Abstract The target article carefully describes the memory system, centered on the temporal lobe that builds specific memory traces. It does not, however, mention the laterality effects that exist within this system. This commentary briefly surveys evidence showing that clear asymmetries exist within the temporal lobe structures subserving the core system and that the right temporal structures mainly underpin face familiarity feelings.

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A scanning electron microscopic study on dissolving process of cholesterol gallstones by chenodeoxycholic acid (CDCA)

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100083485 ◽

1978 ◽

Vol 36 (2) ◽

pp. 522-523

Author(s):

T. Kanetaka ◽

M. Cho ◽

S. Kawamura ◽

T. Sado ◽

K. Hara

Keyword(s):

Electron Microscope ◽

Chenodeoxycholic Acid ◽

Outer Surface ◽

Electron Microscopic ◽

Cholesterol Gallstones ◽

The Core ◽

Scanning Electron Microscopic Study ◽

Scanning Electron Microscopic ◽

Acceleration Voltage ◽

Scanning Electron

The authors have investigated the dissolution process of human cholesterol gallstones using a scanning electron microscope(SEM). This study was carried out by comparing control gallstones incubated in beagle bile with gallstones obtained from patients who were treated with chenodeoxycholic acid(CDCA).The cholesterol gallstones for this study were obtained from 14 patients. Three control patients were treated without CDCA and eleven patients were treated with CDCA 300-600 mg/day for periods ranging from four to twenty five months. It was confirmed through chemical analysis that these gallstones contained more than 80% cholesterol in both the outer surface and the core.The specimen were obtained from the outer surface and the core of the gallstones. Each specimen was attached to alminum sheet and coated with carbon to 100Å thickness. The SEM observation was made by Hitachi S-550 with 20 kV acceleration voltage and with 60-20, 000X magnification.

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The Structure and Development of Microbodies in the Fat Body and other Tissues of an Insect (Calpodes Ethlius)

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010006773x ◽

1970 ◽

Vol 28 ◽

pp. 148-149

Author(s):

M. Locke ◽

J. T. McMahon

Keyword(s):

Electron Microscopy ◽

Liquid Crystals ◽

Fat Body ◽

Competitive Inhibitor ◽

Dense Core ◽

Urate Oxidase ◽

Blood Proteins ◽

Free Base ◽

The Core ◽

The Matrix

The fat body of insects has always been compared functionally to the liver of vertebrates. Both synthesize and store glycogen and lipid and are concerned with the formation of blood proteins. The comparison becomes even more apt with the discovery of microbodies and the localization of urate oxidase and catalase in insect fat body.The microbodies are oval to spherical bodies about 1μ across with a depression and dense core on one side. The core is made of coiled tubules together with dense material close to the depressed membrane. The tubules may appear loose or densely packed but always intertwined like liquid crystals, never straight as in solid crystals (Fig. 1). When fat body is reacted with diaminobenzidine free base and H2O2 at pH 9.0 to determine the distribution of catalase, electron microscopy shows the enzyme in the matrix of the microbodies (Fig. 2). The reaction is abolished by 3-amino-1, 2, 4-triazole, a competitive inhibitor of catalase. The fat body is the only tissue which consistantly reacts positively for urate oxidase. The reaction product is sharply localized in granules of about the same size and distribution as the microbodies. The reaction is inhibited by 2, 6, 8-trichloropurine, a competitive inhibitor of urate oxidase.

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Exsolution and inversion in pigeonite from the Whin Sill, Northern England

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100109513 ◽

1978 ◽

Vol 36 (1) ◽

pp. 474-475

Author(s):

P.P.K. Smith

Keyword(s):

High Temperature ◽

Low Temperature ◽

Homogeneous Nucleation ◽

Silicate Mineral ◽

Antiphase Boundaries ◽

Two Phase ◽

Primitive Form ◽

The Core ◽

Nucleation Mechanisms ◽

And Inversion

Grains of pigeonite, a calcium-poor silicate mineral of the pyroxene group, from the Whin Sill dolerite have been ion-thinned and examined by TEM. The pigeonite is strongly zoned chemically from the composition Wo8En64FS28 in the core to Wo13En34FS53 at the rim. Two phase transformations have occurred during the cooling of this pigeonite:- exsolution of augite, a more calcic pyroxene, and inversion of the pigeonite from the high- temperature C face-centred form to the low-temperature primitive form, with the formation of antiphase boundaries (APB's). Different sequences of these exsolution and inversion reactions, together with different nucleation mechanisms of the augite, have created three distinct microstructures depending on the position in the grain.In the core of the grains small platelets of augite about 0.02μm thick have farmed parallel to the (001) plane (Fig. 1). These are thought to have exsolved by homogeneous nucleation. Subsequently the inversion of the pigeonite has led to the creation of APB's.

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