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Advanced Fluorescence Methodologies: Focus on Macromolecules Research 2.0
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Advanced Fluorescence Methodologies: Focus on Macromolecules Research 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Macromolecules".

Deadline for manuscript submissions: closed (15 March 2024) | Viewed by 2597

Special Issue Editors

Prof. Dr. Joseph P. Albanesi

E-Mail Website
Guest Editor
Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA
Interests: dynamin; phosphoinositides in membrane trafficking; mechanisms of endocytosis and autophagy
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. David M. Jameson

E-Mail Website
Guest Editor
Department of Cell and Molecular Biology, University of Hawaii at Manoa, 651 Ilalo St., BSB222, Honolulu, HI 96813, USA
Interests: fluorescence methods; FLIM/FRET; protein interactions; FCS; polarization/anisotropy
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Detailed analysis of macromolecular structure and dynamics has been greatly facilitated by the use of advanced fluorescence-based experimental approaches. Although the basic principles of fluorescence spectroscopy and imaging were established decades ago, recent conceptual and technological advances have dramatically extended their range of applicability. For example, improvements in optics, electronics, computation, and dye technology have allowed unprecedented access to macromolecular motions and interactions in vitro and in living cells.

This Special Issue will present original research investigations that employ state-of-the-art fluorescence methodologies, as well as review articles that address current progress in the field. Emphasis will be on studies which advance our understanding of biological systems.

Potential topics include, but are not limited to, the following:

  • Fluorescence fluctuation spectroscopy
  • Single-particle tracking
  • Phasor analysis
  • Single-molecule analysis
  • Super-resolution
  • FRET/FLIM
  • Fluorescent probes
  • FRAP

Due to the success of the first edition of this Special Issue, we would like to add more results and new insights from recent research projects.

https://www.mdpi.com/journal/ijms/special_issues/Fluorescence_Methodologies

Prof. Dr. Joseph P. Albanesi
Prof. Dr. David M. Jameson
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • fluorescence
  • FRET
  • FLIM
  • FRAP
  • phasors
  • FCS
  • single molecule
  • super-resolution

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Related Special Issue

Published Papers (2 papers)

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Research

12 pages, 3718 KiB  
Communication
Analysis of Arc/Arg3.1 Oligomerization In Vitro and in Living Cells
by Barbara Barylko, Clinton A. Taylor 4th, Jason Wang, Per Niklas Hedde, Yan Chen, Kwang-Ho Hur, Derk D. Binns, Chad A. Brautigam, George N. DeMartino, Joachim D. Mueller, David M. Jameson and Joseph P. Albanesi
Int. J. Mol. Sci. 2024, 25(12), 6454; https://doi.org/10.3390/ijms25126454 - 12 Jun 2024
Cited by 1 | Viewed by 940
Abstract
Arc (also known as Arg3.1) is an activity-dependent immediate early gene product enriched in neuronal dendrites. Arc plays essential roles in long-term potentiation, long-term depression, and synaptic scaling. Although its mechanisms of action in these forms of synaptic plasticity are not completely well [...] Read more.
Arc (also known as Arg3.1) is an activity-dependent immediate early gene product enriched in neuronal dendrites. Arc plays essential roles in long-term potentiation, long-term depression, and synaptic scaling. Although its mechanisms of action in these forms of synaptic plasticity are not completely well established, the activities of Arc include the remodeling of the actin cytoskeleton, the facilitation of AMPA receptor (AMPAR) endocytosis, and the regulation of the transcription of AMPAR subunits. In addition, Arc has sequence and structural similarity to retroviral Gag proteins and self-associates into virus-like particles that encapsulate mRNA and perhaps other cargo for intercellular transport. Each of these activities is likely to be influenced by Arc’s reversible self-association into multiple oligomeric species. Here, we used mass photometry to show that Arc exists predominantly as monomers, dimers, and trimers at approximately 20 nM concentration in vitro. Fluorescence fluctuation spectroscopy revealed that Arc is almost exclusively present as low-order (monomer to tetramer) oligomers in the cytoplasm of living cells, over a 200 nM to 5 μM concentration range. We also confirmed that an α-helical segment in the N-terminal domain contains essential determinants of Arc’s self-association. Full article
(This article belongs to the Special Issue Advanced Fluorescence Methodologies: Focus on Macromolecules Research 2.0)
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14 pages, 2476 KiB  
Article
A Combination of Library Screening and Rational Mutagenesis Expands the Available Color Palette of the Smallest Fluorogen-Activating Protein Tag nanoFAST
by Nadezhda S. Baleeva, Yulia A. Bogdanova, Marina V. Goncharuk, Anatolii I. Sokolov, Ivan N. Myasnyanko, Vadim S. Kublitski, Alexander Yu. Smirnov, Aidar R. Gilvanov, Sergey A. Goncharuk, Konstantin S. Mineev and Mikhail S. Baranov
Int. J. Mol. Sci. 2024, 25(5), 3054; https://doi.org/10.3390/ijms25053054 - 6 Mar 2024
Cited by 1 | Viewed by 1231
Abstract
NanoFAST is the smallest fluorogen-activating protein, consisting of only 98 amino acids, used as a genetically encoded fluorescent tag. Previously, only a single fluorogen with an orange color was revealed for this protein. In the present paper, using rational mutagenesis and in vitro [...] Read more.
NanoFAST is the smallest fluorogen-activating protein, consisting of only 98 amino acids, used as a genetically encoded fluorescent tag. Previously, only a single fluorogen with an orange color was revealed for this protein. In the present paper, using rational mutagenesis and in vitro screening of fluorogens libraries, we expanded the color palette of this tag. We discovered that E46Q is one of the key substitutions enabling the range of possible fluorogens to be expanded. The introduction of this and several other substitutions has made it possible to use not only orange but also red and green fluorogens with the modified protein. Full article
(This article belongs to the Special Issue Advanced Fluorescence Methodologies: Focus on Macromolecules Research 2.0)
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