LIVIVO - Search results -

Search results

Result 1 - 10 of total 38

Search options

Article ; Online: Complexes of tubulin oligomers and tau form a viscoelastic intervening network cross-bridging microtubules into bundles.

Kohl, Phillip A / Song, Chaeyeon / Fletcher, Bretton J / Best, Rebecca L / Tchounwou, Christine / Garcia Arceo, Ximena / Chung, Peter J / Miller, Herbert P / Wilson, Leslie / Choi, Myung Chul / Li, Youli / Feinstein, Stuart C / Safinya, Cyrus R

Nature communications

2024 Volume 15, Issue 1, Page(s) 2362

Abstract: The axon-initial-segment (AIS) of mature neurons contains microtubule (MT) fascicles (linear bundles) implicated as retrograde diffusion barriers in the retention of MT-associated protein (MAP) tau inside axons. Tau dysfunction and leakage outside of the ...

Abstract	The axon-initial-segment (AIS) of mature neurons contains microtubule (MT) fascicles (linear bundles) implicated as retrograde diffusion barriers in the retention of MT-associated protein (MAP) tau inside axons. Tau dysfunction and leakage outside of the axon is associated with neurodegeneration. We report on the structure of steady-state MT bundles in varying concentrations of Mg
MeSH term(s)	Microtubules/metabolism ; Scattering, Small Angle ; tau Proteins/metabolism ; Tubulin/metabolism ; X-Ray Diffraction ; Humans
Chemical Substances	tau Proteins ; Tubulin ; MAPT protein, human
Language	English
Publishing date	2024-03-15
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-024-46438-x
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Article ; Online: Water Hydrogen-Bond Mediated Layer by Layer Alignment of Lipid Rafts as a Precursor of Intermembrane Processes.

Lee, Suho / Bak, Ji Hyun / Lee, Yuno / Jeong, Dae-Woong / Lee, Jaehee / Lee, KeunMin Ken / Cho, Hasaeam / Lee, Hyun Hwi / Hyeon, Changbong / Choi, Myung Chul

Journal of the American Chemical Society

2024

Abstract: Lipid rafts, which are dynamic nanodomains in the plasma membrane, play a crucial role in intermembrane processes by clustering together and growing in size within the plane of the membrane while also aligning with each other across different membranes. ... ...

Abstract	Lipid rafts, which are dynamic nanodomains in the plasma membrane, play a crucial role in intermembrane processes by clustering together and growing in size within the plane of the membrane while also aligning with each other across different membranes. However, the physical origin of layer by layer alignment of lipid rafts remains to be elucidated. Here, by using fluorescence imaging and synchrotron X-ray reflectivity in a phase-separated multilayer system, we find that the alignment of raft-mimicking L
Language	English
Publishing date	2024-04-23
Publishing country	United States
Document type	Journal Article
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.4c00544
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Bonn / Germany

Z 4' 55/32: Show issues
Z 7.3: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Aggregation and Cellular Toxicity of Pathogenic or Non-pathogenic Proteins.

Lee, Sungmun / Choi, Myung Chul / Al Adem, Kenana / Lukman, Suryani / Kim, Tae-Yeon

Scientific reports

2020 Volume 10, Issue 1, Page(s) 5120

Abstract: More than 20 unique diseases such as diabetes, Alzheimer's disease, Parkinson's disease are caused by the abnormal aggregations of pathogenic proteins such as amylin, β-amyloid (Aβ), and α-synuclein. All pathogenic proteins differ from each other in ... ...

Abstract	More than 20 unique diseases such as diabetes, Alzheimer's disease, Parkinson's disease are caused by the abnormal aggregations of pathogenic proteins such as amylin, β-amyloid (Aβ), and α-synuclein. All pathogenic proteins differ from each other in biological function, primary sequences, and morphologies; however, the proteins are toxic when aggregated. Here, we investigated the cellular toxicity of pathogenic or non-pathogenic protein aggregates. In this study, six proteins were selected and they were incubated at acid pH and high temperature. The aggregation kinetic and cellular toxicity of protein species with time were characterized. Three non-pathogenic proteins, bovine serum albumin (BSA), catalase, and pepsin at pH 2 and 65 °C were stable in protein structure and non-toxic at a lower concentration of 1 mg/mL. They formed aggregates at a higher concentration of 20 mg/mL with time and they induced the toxicity in short incubation time points, 10 min and 20 min only and they became non-toxic after 30 min. Other three pathogenic proteins, lysozyme, superoxide dismutase (SOD), and insulin, also produced the aggregates with time and they caused cytotoxicity at both 1 mg/mL and 20 mg/mL after 10 min. TEM images and DSC analysis demonstrated that fibrils or aggregates at 1 mg/mL induced cellular toxicity due to low thermal stability. In DSC data, fibrils or aggregates of pathogenic proteins had low thermal transition compared to fresh samples. The results provide useful information to understand the aggregation and cellular toxicity of pathogenic and non-pathogenic proteins.
MeSH term(s)	Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/metabolism ; Catalase/metabolism ; Cell Line ; Diabetes Mellitus/genetics ; Diabetes Mellitus/pathology ; Humans ; Insulin/metabolism ; Islet Amyloid Polypeptide/metabolism ; Models, Molecular ; Muramidase/metabolism ; Parkinson Disease/genetics ; Parkinson Disease/pathology ; Pepsin A/metabolism ; Protein Aggregates/physiology ; Protein Aggregation, Pathological/pathology ; Protein Structure, Secondary/physiology ; Serum Albumin, Bovine/metabolism ; Superoxide Dismutase/metabolism ; alpha-Synuclein/metabolism
Chemical Substances	Amyloid beta-Peptides ; Insulin ; Islet Amyloid Polypeptide ; Protein Aggregates ; alpha-Synuclein ; Serum Albumin, Bovine (27432CM55Q) ; Catalase (EC 1.11.1.6) ; Superoxide Dismutase (EC 1.15.1.1) ; Muramidase (EC 3.2.1.17) ; Pepsin A (EC 3.4.23.1)
Language	English
Publishing date	2020-03-20
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-020-62062-3
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Regulation of Interfacial Anchoring Orientation of Anisotropic Nanodumbbells.

Jang, Hyunwoo / Song, Chaeyeon / Kim, Byungsoo / Lee, Chunghyeong / Lee, Juncheol / Han, Youngkyu / An, Ilsin / Kim, Joon Heon / Nam, Jin / Choi, Myung Chul

ACS macro letters

2023 Volume 12, Issue 10, Page(s) 1298–1305

Abstract: Nanoparticles exhibiting geometrical and chemical anisotropies hold promise for environmentally responsive materials with tunable mechanical properties. However, a comprehensive understanding of their interfacial behaviors remains elusive. In this paper, ...

Abstract	Nanoparticles exhibiting geometrical and chemical anisotropies hold promise for environmentally responsive materials with tunable mechanical properties. However, a comprehensive understanding of their interfacial behaviors remains elusive. In this paper, we control the interfacial anchoring orientation of polystyrene nanodumbbells by adjusting interparticle forces. The film nanostructure is characterized by the orientation angle analysis of individual dumbbells from cross-sectional EM data: dumbbells undergo orientation transitions from a distinctive horizontal bilayer to an isotropic anchoring when electrostatic repulsion is suppressed by either an ionic strength increase or surface amine-modification. This anchoring orientation influences the film's mechanical properties and foam stability, as investigated by a 2D isotherm and dark/bright-field microscopy measurements. Our findings highlight the potential for precise control of supra-colloidal structures by modulating particle alignment, paving the way for smart delivery systems.
Language	English
Publishing date	2023-09-11
Publishing country	United States
Document type	Journal Article
ISSN	2161-1653
ISSN (online)	2161-1653
DOI	10.1021/acsmacrolett.3c00339
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Synchrotron X-ray study of intrinsically disordered and polyampholytic Tau 4RS and 4RL under controlled ionic strength.

Cho, Hasaeam / Lee, Jimin / Nho, Hanjoon / Lee, Keunmin / Gim, Bopil / Lee, Juncheol / Lee, Jaehee / Ewert, Kai K / Li, Youli / Feinstein, Stuart C / Safinya, Cyrus R / Jin, Kyeong Sik / Choi, Myung Chul

The European physical journal. E, Soft matter

2023 Volume 46, Issue 9, Page(s) 73

Abstract: Aggregated and hyperphosphorylated Tau is one of the pathological hallmarks of Alzheimer's disease. Tau is a polyampholytic and intrinsically disordered protein (IDP). In this paper, we present for the first time experimental results on the ionic ... ...

Abstract	Aggregated and hyperphosphorylated Tau is one of the pathological hallmarks of Alzheimer's disease. Tau is a polyampholytic and intrinsically disordered protein (IDP). In this paper, we present for the first time experimental results on the ionic strength dependence of the radius of gyration (R
MeSH term(s)	Humans ; X-Rays ; Synchrotrons ; Intrinsically Disordered Proteins
Chemical Substances	Intrinsically Disordered Proteins
Language	English
Publishing date	2023-08-31
Publishing country	France
Document type	Journal Article
ZDB-ID	2004003-9
ISSN	1292-895X ; 1292-8941
ISSN (online)	1292-895X
ISSN	1292-8941
DOI	10.1140/epje/s10189-023-00328-0
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: Inhibition of Human Amylin Aggregation and Cellular Toxicity by Lipoic Acid and Ascorbic Acid.

Azzam, Sarah Kassem / Jang, Hyunwoo / Choi, Myung Chul / Alsafar, Habiba / Lukman, Suryani / Lee, Sungmun

Molecular pharmaceutics

2018 Volume 15, Issue 6, Page(s) 2098–2106

Abstract: More than 30 human degenerative diseases result from protein aggregation such as Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM). Islet amyloid deposits, a hallmark in T2DM, are found in pancreatic islets of more than 90% of T2DM patients. ... ...

Abstract	More than 30 human degenerative diseases result from protein aggregation such as Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM). Islet amyloid deposits, a hallmark in T2DM, are found in pancreatic islets of more than 90% of T2DM patients. An association between amylin aggregation and reduction in β-cell mass was also established by post-mortem studies. A strategy in preventing protein aggregation-related disorders is to inhibit the protein aggregation and associated toxicity. In this study, we demonstrated that two inhibitors, lipoic acid and ascorbic acid, significantly inhibited amylin aggregation. Compared to amylin (15 μM) as 100%, lipoic acid and ascorbic acid reduced amylin fibril formation to 42.1 ± 17.2% and 42.9 ± 12.8%, respectively, which is confirmed by fluorescence and TEM images. In cell viability tests, both inhibitors protected RIN-m5f β-cells from the toxicity of amylin aggregates. At 10:1 molar ratio of lipoic acid to amylin, lipoic acid with amylin increased the cell viability to 70.3%, whereas only 42.8% RIN-m5f β-cells survived in amylin aggregates. For ascorbic acid, an equimolar ratio achieved the highest cell viability of 63.3% as compared to 42.8% with amylin aggregates only. Docking results showed that lipoic acid and ascorbic acid physically interact with amylin amyloidogenic region (residues Ser20-Ser29) via hydrophobic interactions; hence reducing aggregation levels. Therefore, lipoic acid and ascorbic acid prevented amylin aggregation via hydrophobic interactions, which resulted in the prevention of cell toxicity in vitro.
MeSH term(s)	Animals ; Ascorbic Acid/chemistry ; Ascorbic Acid/pharmacology ; Cell Line, Tumor ; Humans ; Hydrophobic and Hydrophilic Interactions ; Islet Amyloid Polypeptide/chemistry ; Islet Amyloid Polypeptide/metabolism ; Molecular Docking Simulation ; Protein Aggregates/drug effects ; Protein Aggregation, Pathological/prevention & control ; Protein Binding ; Rats ; Thioctic Acid/chemistry ; Thioctic Acid/pharmacology
Chemical Substances	Islet Amyloid Polypeptide ; Protein Aggregates ; Thioctic Acid (73Y7P0K73Y) ; Ascorbic Acid (PQ6CK8PD0R)
Language	English
Publishing date	2018-05-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2138405-8
ISSN	1543-8392 ; 1543-8384
ISSN (online)	1543-8392
ISSN	1543-8384
DOI	10.1021/acs.molpharmaceut.7b01009
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 6250: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Enhanced stability of freestanding lipid bilayer and its stability criteria.

Jeong, Dae-Woong / Jang, Hyunwoo / Choi, Siyoung Q / Choi, Myung Chul

Scientific reports

2016 Volume 6, Page(s) 38158

Abstract: We present a new strategy to dramatically enhance the stability of freestanding lipid bilayers. We found that an addition of a water in oil emulsion stabilizer, SPAN 80 to a solvent phase guarantees nearly millimeter-scale stable freestanding lipid ... ...

Abstract	We present a new strategy to dramatically enhance the stability of freestanding lipid bilayers. We found that an addition of a water in oil emulsion stabilizer, SPAN 80 to a solvent phase guarantees nearly millimeter-scale stable freestanding lipid bilayers. The water permeability, bilayer area, contact angle, and interfacial tension were measured as a function of time and SPAN 80-to-lipid weight ratio (Φ
MeSH term(s)	Dimyristoylphosphatidylcholine/chemistry ; Hexoses/chemistry ; Lipid Bilayers/chemistry ; Models, Chemical ; Phosphatidylcholines/chemistry
Chemical Substances	Hexoses ; Lipid Bilayers ; Phosphatidylcholines ; sorbitan monooleate (06XEA2VD56) ; 1,2-oleoylphosphatidylcholine (EDS2L3ODLV) ; Dimyristoylphosphatidylcholine (U86ZGC74V5)
Language	English
Publishing date	2016-12-16
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/srep38158
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Fluorescence Recovery after Merging a Droplet to Measure the Two-dimensional Diffusion of a Phospholipid Monolayer.

Jeong, Dae-Woong / Kim, KyuHan / Choi, Myung Chul / Choi, Siyoung Q

Journal of visualized experiments : JoVE

2015 , Issue 105, Page(s) e53376

Abstract: We introduce a new method to measure the lateral diffusivity of a surfactant monolayer at the fluid-fluid interface, called fluorescence recovery after merging (FRAM). FRAM adopts the same principles as the fluorescence recovery after photobleaching ( ... ...

Abstract	We introduce a new method to measure the lateral diffusivity of a surfactant monolayer at the fluid-fluid interface, called fluorescence recovery after merging (FRAM). FRAM adopts the same principles as the fluorescence recovery after photobleaching (FRAP) technique, especially for measuring fluorescence recovery after bleaching a specific area, but FRAM uses a drop coalescence instead of photobleaching dye molecules to induce a chemical potential gradient of dye molecules. Our technique has several advantages over FRAP: it only requires a fluorescence microscope rather than a confocal microscope equipped with high power lasers; it is essentially free from the selection of fluorescence dyes; and it has far more freedom to define the measured diffusion area. Furthermore, FRAM potentially provides a route for studying the mixing or inter-diffusion of two different surfactants, when the monolayers at a surface of droplet and at a flat air/water interface are prepared with different species, independently.
MeSH term(s)	Diffusion ; Fluorescence Recovery After Photobleaching/methods ; Microscopy, Fluorescence ; Phospholipids/chemistry ; Photobleaching ; Surface-Active Agents/chemistry ; Water/chemistry
Chemical Substances	Phospholipids ; Surface-Active Agents ; Water (059QF0KO0R)
Language	English
Publishing date	2015-10-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Video-Audio Media
ISSN	1940-087X
ISSN (online)	1940-087X
DOI	10.3791/53376
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Full text

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- Full text online
- Order with fees

Article: Minireview - Microtubules and Tubulin Oligomers: Shape Transitions and Assembly by Intrinsically Disordered Protein Tau and Cationic Biomolecules

Safinya, Cyrus R / Chung, Peter J / Song, Chaeyeon / Li, Youli / Miller, Herbert P / Choi, Myung Chul / Raviv, Uri / Ewert, Kai K / Wilson, Leslie / Feinstein, Stuart C

Langmuir. 2019 Sept. 20, v. 35, no. 48

2019

Abstract: In this minireview, which is part of a special issue in honor of Jacob N. Israelachvili’s remarkable research career on intermolecular forces and interfacial science, we present studies of structures, phase behavior, and forces in reaction mixtures of ... ...

Abstract	In this minireview, which is part of a special issue in honor of Jacob N. Israelachvili’s remarkable research career on intermolecular forces and interfacial science, we present studies of structures, phase behavior, and forces in reaction mixtures of microtubules (MTs) and tubulin oligomers with either intrinsically disordered protein (IDP) Tau, cationic vesicles, or the polyamine spermine (4+). Bare MTs consist of 13 protofilaments (PFs), on average, where each PF is made of a linear stack of αβ-tubulin dimers (i.e., tubulin oligomers). We begin with a series of experiments which demonstrate the flexibility of PFs toward shape changes in response to local environmental cues. First, studies show that MT-associated protein (MAP) Tau controls the diameter of microtubules upon binding to the outer surface, implying a shape change in the cross-sectional area of PFs forming the MT perimeter. The diameter of a MT may also be controlled by the charge density of a lipid bilayer membrane that coats the outer surface. We further describe an experimental study where it is unexpectedly found that the biologically relevant polyamine spermine (+4e) is able to depolymerize taxol-stabilized microtubules with efficiency that increases with decreasing temperature. This MT destabilization drives a dynamical structural transition where inside-out curving of PFs, during the depolymerization peeling process, is followed by reassembly of ring-like curved PF building blocks into an array of helical inverted tubulin tubules. We finally turn to a very recent study on pressure–distance measurements in bundles of MTs employing the small-angle X-ray scattering (SAXS)-osmotic pressure technique, which complements the surface-forces-apparatus technique developed by Jacob N. Israelachvili. These latter studies are among the very few which are beginning to shed light on the precise nature of the interactions between MTs mediated by MAP Tau in 37 °C reaction mixtures containing GTP and lacking taxol.
Keywords	depolymerization ; guanosine triphosphate ; lipid bilayers ; microtubules ; paclitaxel ; peeling ; small-angle X-ray scattering ; spermine ; temperature ; tubulin
Language	English
Dates of publication	2019-0920
Size	p. 15970-15978.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	2005937-1
ISSN	1520-5827 ; 0743-7463
ISSN (online)	1520-5827
ISSN	0743-7463
DOI	10.1021/acs.langmuir.9b02208
Database	NAL-Catalogue (AGRICOLA)

Order via subito

Article: Fluorescence recovery after merging a droplet to measure the two-dimensional diffusion of a phospholipid monolayer

Jeong, Dae-Woong / Kim, KyuHan / Choi, Myung Chul / Choi, Siyoung Q

Journal of visualized experiments. 2015 Oct. 15, , no. 104

2015

Abstract	We introduce a new method to measure the lateral diffusivity of a surfactant monolayer at the fluid-fluid interface, called fluorescence recovery after merging (FRAM). FRAM adopts the same principles as the fluorescence recovery after photobleaching (FRAP) technique, especially for measuring fluorescence recovery after bleaching a specific area, but FRAM uses a drop coalescence instead of photobleaching dye molecules to induce a chemical potential gradient of dye molecules. Our technique has several advantages over FRAP: it only requires a fluorescence microscope rather than a confocal microscope equipped with high power lasers; it is essentially free from the selection of fluorescence dyes; and it has far more freedom to define the measured diffusion area. Furthermore, FRAM potentially provides a route for studying the mixing or inter-diffusion of two different surfactants, when the monolayers at a surface of droplet and at a flat air/water interface are prepared with different species, independently.
Keywords	air ; bleaching ; diffusivity ; droplets ; fluorescence ; fluorescence microscopes ; fluorescence recovery after photobleaching ; fluorescent dyes ; lasers ; mixing ; phospholipids ; photobleaching ; surfactants
Language	English
Dates of publication	2015-1015
Size	p. e53376.
Publishing place	Journal of Visualized Experiments
Document type	Article
ZDB-ID	2259946-0
ISSN	1940-087X
ISSN	1940-087X
DOI	10.3791/53376
Database	NAL-Catalogue (AGRICOLA)

Order via subito

To top

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito