Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
8.1
4.9
Journals
IJMS
Special Issues
Protein Structure-Function Relationships and Inhibition: From Molecular Insights to Therapeutic...
ijms-logo
Submit to IJMS Review for IJMS Propose a Special Issue

Journal Menu

► Journal Menu

Journal Browser

► Journal Browser
share announcement

Protein Structure-Function Relationships and Inhibition: From Molecular Insights to Therapeutic Applications

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

Deadline for manuscript submissions: closed (30 April 2024) | Viewed by 419

Special Issue Editors

Dr. Nicole Balasco

E-Mail Website
Guest Editor
Institute of Molecular Biology and Pathology, National Research Council (CNR), Department of Chemistry, University of Rome Sapienza, Piazzale Aldo Moro 5, 00185 Rome, Italy
Interests: protein structure–function; molecular modeling; molecular dynamics; molecular interactions; computational biology; structural biology
Special Issues, Collections and Topics in MDPI journals
Dr. Luigi Vitagliano

E-Mail Website
Guest Editor
Institute of Biostructures and Bioimaging, CNR, Via Pietro Castellino n. 111, 80131 Napoli, Italy
Interests: protein structure–function; molecular dynamics; computational biology; structural biology; molecular basis of diseases; biophysics
Special Issues, Collections and Topics in MDPI journals
Dr. Antonella Paladino

E-Mail Website
Guest Editor
Institute of Biostructures and Bioimaging, CNR, Via Pietro Castellino n. 111, 80131 Napoli, Italy
Interests: computational biology and chemistry; structural modeling; molecular dynamics; docking; PPI; molecular interactions; protein structure/function
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Proteins are central players in all biological processes. A fundamental paradigm of structural biology assumes that the functionality of these macromolecules is strictly related to their three-dimensional structures. In this scenario, the understanding of protein structures is a prerequisite for modulating their activities and for developing new therapeutic agents targeting these giant biomolecules. The acquisition of atomic-level structural information about proteins is also fundamental for their modulation. For decades, this task has been extremely difficult due to the complex and time-consuming methodologies utilized to obtain experimental structural data. Very recently, the introduction of effective machine-learning-based approaches, such as Alpha Fold, has provided accurate structural information about proteins, starting from their amino acid sequences. This represents an extremely useful tool for the development of novel molecular entities aimed at enhancing or impairing protein functions.

We encourage the submission of original contributions, short communications, or review articles that describe the development and application of computational and experimental structural biology techniques in order to foster drug development and optimization.

Dr. Nicole Balasco
Dr. Luigi Vitagliano
Dr. Antonella Paladino
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

  • protein structure determination
  • protein folding
  • protein function–structure relationships
  • protein function modulation
  • protein structure–stability
  • protein structure predictions
  • structure-based drug design (SBDD)
  • drug optimization

Published Papers (1 paper)

Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

20 pages, 5750 KiB  
Article
Structure-Function Insights into the Dual Role in Nucleobase and Nicotinamide Metabolism and a Possible Use in Cancer Gene Therapy of the URH1p Riboside Hydrolase
by Alejandra Angela Carriles, Laura Muzzolini, Claudia Minici, Paola Tornaghi, Marco Patrone and Massimo Degano
Int. J. Mol. Sci. 2024, 25(13), 7032; https://doi.org/10.3390/ijms25137032 - 27 Jun 2024
Viewed by 187
Abstract
The URH1p enzyme from the yeast Saccharomyces cerevisiae has gained significant interest due to its role in nitrogenous base metabolism, particularly involving uracil and nicotinamide salvage. Indeed, URH1p was initially classified as a nucleoside hydrolase (NH) with a pronounced preference for uridine substrate [...] Read more.
The URH1p enzyme from the yeast Saccharomyces cerevisiae has gained significant interest due to its role in nitrogenous base metabolism, particularly involving uracil and nicotinamide salvage. Indeed, URH1p was initially classified as a nucleoside hydrolase (NH) with a pronounced preference for uridine substrate but was later shown to also participate in a Preiss-Handler-dependent pathway for recycling of both endogenous and exogenous nicotinamide riboside (NR) towards NAD+ synthesis. Here, we present the detailed enzymatic and structural characterisation of the yeast URH1p enzyme, a member of the group I NH family of enzymes. We show that the URH1p has similar catalytic efficiencies for hydrolysis of NR and uridine, advocating a dual role of the enzyme in both NAD+ synthesis and nucleobase salvage. We demonstrate that URH1p has a monomeric structure that is unprecedented for members of the NH homology group I, showing that oligomerisation is not strictly required for the N-ribosidic activity in this family of enzymes. The size, thermal stability and activity of URH1p towards the synthetic substrate 5-fluoruridine, a riboside precursor of the antitumoral drug 5-fluorouracil, make the enzyme an attractive tool to be employed in gene-directed enzyme-prodrug activation therapy against solid tumours. Full article
(This article belongs to the Special Issue Protein Structure-Function Relationships and Inhibition: From Molecular Insights to Therapeutic Applications)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-1
Back to TopTop