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Modulatory Mutagenic Impacts on Photo-/Biophysical Performance of Fluorescent Proteins

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

Deadline for manuscript submissions: closed (15 May 2024) | Viewed by 236

Special Issue Editor

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Guest Editor
Molecular Imaging Program at Stanford (MIPS), Departments of Radiology (Interventional) and Otolaryngology - Head/Neck Surgery, Stanford University School of Medicine, Stanford, CA, USA
Interests: molecular imaging; nanoparticles; drug delivery; immunotherapy; glioblastoma; affi-/nanobody; bio-/molecular probes and sensors; fluorescence-guided surgery; near-infrared I/II fluorescence; image-guided surgery; surgical navigational technology; directed enzyme prodrug therapy (DEPT)
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Special Issue Information

Dear Colleagues,

Endogenous and transfected expressed fluorogenic proteins in either their unadulterated (native) or genetically-modified tailored (bioengineered) form, such as hemoglobin, select phyla-originating species-based domains (e.g., that of which affords green fluorescent protein, GFP), and mRaspberry, have all been exploited as optical markers or modulable reporters conferring the capability(-ies) of affording the visual identification, monitoring, and/or discernment of a host of intercellular signaling activities, intra-/extracellular biological processes, and structural/conformational reshaping, with high spatiotemporal resolutions in life sciences research and biomedical applications especially upon the facilitation of induction events, by providing permanently “ON”, togglable “OFF-0N” as well as “ON-OFF”, and blinking “OFF-ON” peak fluorescence emission at discrete wavelengths that collectively span the visible (ca. 405–700 nm) and near-infrared-I (NIR-I, ca. 700–1000 nm) spectral imaging windows following transient photoirradiation-induced (i) promotion of their electronics into an excited state of higher energetics and (ii) geometrical distortion(s) or rearrangement(s). To allow for such, highly-specific interactions between and modification(s) to the underlying amino acid sequence backbone of a given fluorogenic construct itself and/or to the multidirectional/-functional co-interacting species about its periphery are necessary, all of which can arise from (i) compositional alterations to the originating DNA via such undergoing spontaneous pinpoint mutations and/or single/multi site-directed substitutions, (ii) post-translation modifications, and/or (iv) any combination thereof. Thus, these actions alter the innate structural and fluorescent properties of such types of proteins at both their proprotein and mature state. Accordingly, the purpose and scope of this Special Issue is to serve as a forum to facilitate the communication of new research findings and sound insights derived thereof obtained from conventional and innovative investigative efforts arising from noteworthy research initiatives that peer into and assess the impact of modifications to fluorescent proteins on the experimentally-determined resultant structural, functional, and photophysical effects from a holistic system-wide perspective as well as the fine interplay between such from a micro perspective level.

Dr. Kenneth S. Hettie
Guest Editor

Manuscript Submission Information

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  • fluorescent protein
  • molecular imaging
  • near-infrared fluorescence (NIR)
  • protein bioengineering
  • optical reporter

Published Papers

There is no accepted submissions to this special issue at this moment.
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