Fibie a 28 ans
![](/file/3811b1f5dcd37f27f628d.gif)
⚡ TOUTES LES INFORMATIONS CLIQUEZ ICI 👈🏻👈🏻👈🏻
Fibie a 28 ans
Clipboard, Search History, and several other advanced features are temporarily unavailable.
Dashboard
Publications
Account settings
Log out
Advanced
Clipboard
Format
Abstract
PubMed
PMID
Format:
Summary (text)
PubMed
PMID
Abstract (text)
CSV
Subject:
1 selected item: 32008441 - PubMed
Format:
Summary
Summary (text)
Abstract
Abstract (text)
Create a new collection
Add to an existing collection
Name must be less than 100 characters
Unable to load your collection due to an error
Please try again
Unable to load your delegates due to an error
Please try again
Would you like email updates of new search results?
Saved Search Alert Radio Buttons
Yes
No
Frequency:
Monthly
Weekly
Daily
Which day?
The first Sunday
The first Monday
The first Tuesday
The first Wednesday
The first Thursday
The first Friday
The first Saturday
The first day
The first weekday
Which day?
Sunday
Monday
Tuesday
Wednesday
Thursday
Friday
Saturday
Report format:
Summary
Summary (text)
Abstract
Abstract (text)
PubMed
Send at most:
1 item
5 items
10 items
20 items
50 items
100 items
200 items
Send even when there aren't any new results
Number of items displayed:
5
10
15
20
50
100
Page navigation
Title & authors
Abstract
Figures
Similar articles
Cited by
References
Publication types
MeSH terms
Substances
Related information
Grant support
LinkOut - more resources
Affiliations
1 Laboratory of Cell Morphology, Institute of Cytology Russian Academy of Science, St. Petersburg, Russia.
2 Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology Russian Academy of Science, St. Petersburg, Russia.
3 Institute of Physics, Nanotechnology and Telecommunications, Peter the Great St. Petersburg Polytechnic University, St. Petersburg, Russia.
M I Sulatsky et al.
Prion .
2020 Dec .
Format
Abstract
PubMed
PMID
Affiliations
1 Laboratory of Cell Morphology, Institute of Cytology Russian Academy of Science, St. Petersburg, Russia.
2 Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology Russian Academy of Science, St. Petersburg, Russia.
3 Institute of Physics, Nanotechnology and Telecommunications, Peter the Great St. Petersburg Polytechnic University, St. Petersburg, Russia.
Morphology and staining by fluorescent probes of amyloid fibrils formed from lysozyme (top panels) and insulin (bottom panels) using of buffer solution with pH 6.3. Left panels show transmission electron microscopy (TEM) images of amyloid fibrils in the absence (AF) and in the presence of fluorescent probes ANS (AF+ANS) and ThT (AF+ThT). Data of confocal laser scanning microscopy (CLSM, Right panels) show amyloids stained by these fluorescent probes. The scale bars on the TEM and CLSM images are equal to 1 and 4 µm, respectively.
Photophysical properties of amyloid fibrils formed from lysozyme and insulin using of buffer solution with pH 6.3 and their binding to fluorescent probes ThT and ANS. (a) -Rayleigh Light Scattering (RLS) and (b) – turbidity (at λ = 530 nm) of amyloids. (c) – normalized absorbance and (d) – fluorescence spectra of ANS in free (ANS) and bound to lysozyme (Lys+ANS) and insulin (Ins+ANS) amyloid fibrils states. (e) – normalized absorbance and (f) – fluorescence spectra of ThT in free (ThT) and bound to lysozyme (Lys+ThT) and insulin (Ins+ThT) amyloid fibrils states. CD spectra of (g) lysozyme and (h) insulin amyloid fibrils in the absence (Lys, Ins) and in the presence of fluorescent probes ANS (Lys+ANS, Ins+ANS) and ThT (Lys+ThT, Ins+ThT).
Morphology and photophysical properties of ultrasonicated amyloid fibrils formed from lysozyme and insulin using of buffer solution with pH 6.3 and and their binding to fluorescent probes ThT and ANS. (a), (b) – transmission electron microscopy (TEM) images of amyloid fibrils formed from lysozyme and insulin, respectively, before and after ultrasonication. The scale bars on the images are equal to 500 nm. (c) – normalized absorbance spectra of ANS in free (ANS) and bound to lysozyme (Lys+ANS) and insulin (Ins+ANS) amyloid fibrils states. (d) – normalized absorbance spectra of ThT in free (ThT) and bound to lysozyme (Lys+ThT) and insulin (Ins+ThT) amyloid fibrils states. (e) – Rayleigh Light Scattering (RLS) and (f) turbidity (at λ = 530 nm) of amyloids. CD spectra of (g) lysozyme and (h) insulin amyloid fibrils in the absence (Lys, Ins) and in the presence of fluorescent probes ANS (Lys+ANS, Ins+ANS) and ThT (Lys+ThT, Ins+ThT).
Morphology and staining by fluorescent probes of amyloid fibrils formed from lysozyme (top panels) and insulin (bottom panels) using of buffer solution with pH 2. Left panels show transmission electron microscopy (TEM) images of amyloid fibrils in the absence (AF) and in the presence of fluorescent probes ANS (AF+ANS) and ThT (AF+ThT). Data of confocal laser scanning microscopy images (CLSM, Right panels) show amyloids stained by these fluorescent probes. The scale bars on the TEM and CLSM images are equal to 1 and 4 µm, respectively.
Photophysical properties of amyloid fibrils formed from lysozyme and insulin using of buffer solution with pH 2 and their binding to fluorescent probes ThT and ANS. (a) – Rayleigh Light Scattering (RLS) and (b) – turbidity (at λ = 530 nm) of amyloids. (c) – normalized absorbance and (d) – fluorescence spectra of ANS in free (ANS) and bound to lysozyme (Lys+ANS) and insulin (Ins+ANS) amyloid fibrils states. (e) – normalized absorbance and (f) fluorescence spectra of ThT in free (ThT) and bound to lysozyme (Lys+ThT) and insulin (Ins+ThT) amyloid fibrils states. CD spectra of (g) lysozyme and (h) insulin amyloid fibrils in the absence (Lys, Ins) and in the presence of fluorescent probes ANS (Lys+ANS, Ins+ANS) and ThT (Lys+ThT, Ins+ThT).
Stepanenko OV, Sulatsky MI, Mikhailova EV, Stepanenko OV, Kuznetsova IM, Turoverov KK, Sulatskaya AI.
Stepanenko OV, et al.
Int J Mol Sci. 2021 May 2;22(9):4828. doi: 10.3390/ijms22094828.
Int J Mol Sci. 2021.
PMID: 34063223
Free PMC article.
Ziaunys M, Smirnovas V.
Ziaunys M, et al.
J Phys Chem B. 2019 Oct 17;123(41):8727-8732. doi: 10.1021/acs.jpcb.9b08652. Epub 2019 Oct 8.
J Phys Chem B. 2019.
PMID: 31580671
Sulatskaya AI, Rodina NP, Polyakov DS, Sulatsky MI, Artamonova TO, Khodorkovskii MA, Shavlovsky MM, Kuznetsova IM, Turoverov KK.
Sulatskaya AI, et al.
Int J Mol Sci. 2018 Sep 14;19(9):2762. doi: 10.3390/ijms19092762.
Int J Mol Sci. 2018.
PMID: 30223436
Free PMC article.
Biancalana M, Koide S.
Biancalana M, et al.
Biochim Biophys Acta. 2010 Jul;1804(7):1405-12. doi: 10.1016/j.bbapap.2010.04.001. Epub 2010 Apr 22.
Biochim Biophys Acta. 2010.
PMID: 20399286
Free PMC article.
Review.
Verma S, Ravichandiran V, Ranjan N.
Verma S, et al.
Biochimie. 2021 Nov;190:111-123. doi: 10.1016/j.biochi.2021.06.003. Epub 2021 Jun 9.
Biochimie. 2021.
PMID: 34118329
Review.
Onchaiya S, Saotome T, Mizutani K, Martinez JC, Tame JRH, Kidokoro SI, Kuroda Y.
Onchaiya S, et al.
Molecules. 2022 Apr 28;27(9):2813. doi: 10.3390/molecules27092813.
Molecules. 2022.
PMID: 35566161
Free PMC article.
Vignon A, Salvador-Prince L, Lehmann S, Perrier V, Torrent J.
Vignon A, et al.
Int J Mol Sci. 2021 Aug 16;22(16):8769. doi: 10.3390/ijms22168769.
Int J Mol Sci. 2021.
PMID: 34445475
Free PMC article.
Review.
Zuo R, Liu R, Olguin J, Hudalla GA.
Zuo R, et al.
J Phys Chem B. 2021 Jun 24;125(24):6559-6571. doi: 10.1021/acs.jpcb.1c02083. Epub 2021 Jun 15.
J Phys Chem B. 2021.
PMID: 34128680
Free PMC article.
Stepanenko OV, Sulatsky MI, Mikhailova EV, Stepanenko OV, Kuznetsova IM, Turoverov KK, Sulatskaya AI.
Stepanenko OV, et al.
Int J Mol Sci. 2021 May 2;22(9):4828. doi: 10.3390/ijms22094828.
Int J Mol Sci. 2021.
PMID: 34063223
Free PMC article.
Obstarczyk P, Lipok M, Grelich-Mucha M, Samoć M, Olesiak-Bańska J.
Obstarczyk P, et al.
J Phys Chem Lett. 2021 Feb 11;12(5):1432-1437. doi: 10.1021/acs.jpclett.0c03511. Epub 2021 Feb 1.
J Phys Chem Lett. 2021.
PMID: 33522819
Free PMC article.
This work was supported by grant from Russian Science Foundation № 18-74-10100 (experiments with lysozyme amyloids), RF President Fellowships SP-841.2018.4 (experiments with insulin amyloids) and SP-259.2019.4 (analysis of ANS binding to monomeric proteins).
Format:
AMA
APA
MLA
NLM
Send To
Clipboard
Email
Save
My Bibliography
Collections
Citation Manager
[x]
NLM
NIH
HHS
USA.gov
An official website of the United States government
The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before
sharing sensitive information, make sure you’re on a federal
government site.
The site is secure.
The https:// ensures that you are connecting to the
official website and that any information you provide is encrypted
and transmitted securely.
Fluorescent probes thioflavin T (ThT) and 1-anilino-8-naphthalene sulfonate (ANS) are widely used to study amyloid fibrils that accumulate in the body of patients with serious diseases, such as Alzheimer's, Parkinson's, prion diseases, etc. However, the possible effect of these probes on amyloid fibrils is not well understood. In this work, we investigated the photophysical characteristics, structure, and morphology of mature amyloid fibrils formed from two model proteins, insulin and lysozyme, in the presence of ThT and ANS. It turned out that ANS affects the secondary structure of amyloids (shown for fibrils formed from insulin and lysozyme) and their fibers clusterization (valid for lysozyme fibrils), while ThT has no such effects. These results confirm the differences in the mechanisms of these dyes interaction with amyloid fibrils. Observed effect of ANS was explained by the electrostatic interactions between the dye molecule and cationic groups of amyloid-forming proteins (unlike hydrophobic binding of ThT) that induce amyloids conformational changes. This interaction leads to weakening repulsion between positive charges of amyloid fibrils and can promote their clusterization. It was shown that when fibrillogenesis conditions and, consequently, fibrils structure is changing, as well as during defragmentation of amyloids by ultrasonication, the influence of ANS to amyloids does not change, which indicates the universality of the detected effects. Based on the obtained results, it was concluded that ANS should be used cautiously for the study of amyloid fibrils, since this fluorescence probe have a direct effect on the object of study.
Keywords:
1-anilino-8-naphthalene sulfonate (ANS); Amyloid fibrils; fluorescent probes; morphology; secondary structure; thioflavin T (ThT); ultrasonication.
Morphology and staining by fluorescent…
Morphology and staining by fluorescent probes of amyloid fibrils formed from lysozyme (top…
Photophysical properties of amyloid fibrils…
Photophysical properties of amyloid fibrils formed from lysozyme and insulin using of buffer…
Morphology and photophysical properties of…
Morphology and photophysical properties of ultrasonicated amyloid fibrils formed from lysozyme and insulin…
Morphology and staining by fluorescent…
Morphology and staining by fluorescent probes of amyloid fibrils formed from lysozyme (top…
Photophysical properties of amyloid fibrils…
Photophysical properties of amyloid fibrils formed from lysozyme and insulin using of buffer…
MeSH
PMC
Bookshelf
Disclaimer
Help
Accessibility
Careers
Obtenir le lien
Facebook
Twitter
Pinterest
E-mail
Autres applications
Inscription au blog et/ou à la newsletter :
Obtenir le lien
Facebook
Twitter
Pinterest
E-mail
Autres applications
Obtenir le lien
Facebook
Twitter
Pinterest
E-mail
Autres applications
Obtenir le lien
Facebook
Twitter
Pinterest
E-mail
Autres applications
Famille nomade à vélo
Depuis 2010 nous sommes nomades sur les routes du monde.
De la Chine à l'Alaska, de la Syrie à la Nouvelle-Zélande. Nos deux filles sont nées en chemin. Nayla a appris à marcher face aux temples d'Angkor. Fibie a fait ses premiers dans une yourte en Mongolie.
Consulter le profil
Nous avons été appelés en Suisse, nous le
sentons. Présenter la Suisse à Fibie, ainsi
que sa famille, serrer ceux que l’on aime
contre nos cœurs, faisaient partie de ce
passage. Nous avons aussi ressenti que
nous étions là pour transmettre. C’est ainsi
que nous avons donnés des ateliers et plus
de 35 conférences en à peine trois mois.
Ces conférences étaient une invitation à
plonger dans l’inconnu.
Nous y avons parlé de la peur. De la peur du premier
pas vers la vie qui vibre pour nous et surtout des
peurs intérieures que nous portons en chacun de nous.
Si les participants sont arrivés avec des questions
plein la tête, ils sont repartis avec des questions plein
le cœur, selon les témoignages que nous avons reçus.
Nous sentons alors que nous ouvrons une nouvelle
porte. Nos expériences en tant que nomades en
famille ne sont pas uniquement une initiation
personnelle, en les partageant, elles deviennent des
initiations pour d’autres. Nayla et Fibie participeront
aussi à parler en public, chanter en chinois ou dire
quelques mots en japonais. Nayla prendra la parole
pour répondre aux questions, dans une aisance
remarquable.
Nous partageons alors nos dernières
conférences à Grindelwald et à Zermatt. Nous
terminons ainsi ces quelques mois face à l’Eiger et au
Cervin dans les prairies alpines recouvertes de fleurs
sauvages. Fibie, qui n’a pas encore 5 ans, marche
dans les petits sentiers pédestres, dévalant les pentes
ou courant vers les sommets pendant 6 heures. Les
paysages suisses sont éblouissants, une pureté s’y
dévoile. Toutes ces explorations nous ont permis de
nous relier à l’énergie de la Terre suisse, de sa source
d’inspiration et d’élévation.
____________ ____________ ____________ _______
From Wikipedia, the free encyclopedia
This is the latest accepted revision , reviewed on 18 August 2022 .
Kira Kosarin
Jack Griffo
Addison Riecke
Diego Velazquez
Chris Tallman
Rosa Blasi
Maya Le Clark
Jed Spingarn
Dan Cross & David Hoge
Sean W. Cunningham & Marc Dworkin
Cross Hoge Productions
Nickelodeon Productions
Dworkingham Productions
^ Due to the duration of this episode, it leaked into Nick at Nite , which spli
Coquine avec un gros cul se prend une bite
Belle brunette baisée par un noir
Aleska Diamond en bouffeuse de chatte - Video porno films xxx sexe en streaming