488 results match your criteria: "Institute for Biological Instrumentation[Affiliation]"

Consortium of 2029 and 7247 Strains Shows In Vitro Bactericidal Effect on and, in Combination with Prebiotic, Protects Against Intestinal Barrier Dysfunction.

Antibiotics (Basel)

November 2024

Department of Biomolecular Sciences, School of Life Sciences, Chemistry and Pharmacy, Faculty of Health, Science, Social Care and Education, Kingston University London, Kingston upon Thames KT1 2EE, UK.

(CJ) is the etiological agent of the world's most common intestinal infectious food-borne disease, ranging from mild symptoms to fatal outcomes. The development of innovative synbiotics that inhibit the adhesion and reproduction of multidrug-resistant (MDR) CJ in animals and humans, thereby preserving intestinal homeostasis, is relevant. We have created a synbiotic based on the consortium of 2029 (LC2029), 7247 (LS7247), and a mannan-rich prebiotic (Actigen).

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Cells of the methylotrophic yeast Ogataea parapolymorpha have two genes encoding low-affinity phosphate transporters: PHO87, encoding the plasma membrane transporter, and PHO91, encoding a protein, which is homologous to the Saccharomyces cerevisiae vacuolar membrane transporter. Earlier, we reported that inactivation of PHO91 in O. parapolymorpha interferes with methanol utilization due to the lack of activity of methanol oxidase encoded by the MOX gene.

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X-ray-induced photodynamic therapy (X-PDT) represents a promising new method of cancer treatment. A novel type of nanoscintillator based on cerium fluoride (CeF) nanoparticles (NPs) modified with flavin mononucleotide (FMN) has been proposed. A method for synthesizing CeF-FMN NPs has been developed, enabling the production of colloidal, spherical NPs with an approximate diameter of 100 nm, low polydispersity, and a high fluorescence quantum yield of 0.

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The RNA-binding S1 domain is a β-barrel with a highly conserved RNA-binding site on its surface. This domain is an important part of the structures of different bacterial, archaeal, and eukaryotic proteins. A distinctive feature of the S1 domain is multiple presences (structural repeats) in proteins and protein complexes.

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Autoimmune uveitis is a relapsing blind-causing ocular condition with complex pathogenesis that is not completely understood. There is a high demand for accurate animal models of experimental autoimmune uveitis (EAU) suitable for elucidating the molecular mechanisms of the disease and testing new therapeutic approaches. Here, we demonstrated that photoreceptor Ca/Zn-sensor protein recoverin is a uveoretinal antigen in albino rabbits provoking typical autoimmune chorioretinitis 2-4 weeks after immunization.

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A Novel Subsp. T1 Strain from Cow's Milk: Homeostatic and Antibacterial Activity against ESBL-Producing .

Antibiotics (Basel)

September 2024

Department of Biomolecular Sciences, School of Life Sciences, Chemistry and Pharmacy, Faculty of Health, Science, Social Care and Education, Kingston University London, Kingston upon Thames KT1 2EE, UK.

The global emergence of antibiotic-resistant zooanthroponotic strains, producing extended-spectrum beta-lactamases (ESBL-E) and persisting in the intestines of farm animals, has now led to the development of a pandemic of extra-intestinal infectious diseases in humans. The search for innovative probiotic microorganisms that eliminate ESBL-E from the intestines of humans and animals is relevant. Previously, we received three isolates of bifidobacteria: from milk of a calved cow (BLLT1), feces of a newborn calf (BLLT2) and feces of a three-year-old child who received fresh milk from this calved cow (BLLT3).

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Intellectual disability and autistic features are associated with chromosome region 2q23.q23.2 duplication carrying LYPD6 and LYPD6B genes.

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Article Synopsis
  • Scientists are studying a special protein from a tiny animal called the tardigrade to learn how it can survive tough conditions and use that knowledge for medicine and space research.
  • The protein, named Dsup, helps protect DNA from damage caused by harmful things, like radiation.
  • Researchers discovered that Dsup has a flexible structure and can sort of "hug" DNA in a loose way, which helps keep it safe.
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Small-angle X-ray scattering (SAXS) and Fourier transform infrared (FTIR) spectroscopy were used to investigate structural peculiarities of two types of amyloid aggregates of smooth muscle titin, which differed in their morphology and ability to disaggregate, and differently bound thioflavin T dye. SAXS showed that the structure/shape of the two titin aggregate types was close to a flat shape. FTIR spectroscopy revealed no differences in the secondary structure of the two types.

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Article Synopsis
  • Solvatochromic compounds are useful probes for biological research, specifically for tracking changes in protein structures.
  • The study utilized thiol-reactive solvatochromic analogs of the GFP chromophore to monitor two proteins: recoverin and the A adenosine receptor (AAR), finding that the best dye (DyeC) showed significant fluorescence changes related to protein activation.
  • The research highlights the potential of GFP-inspired dyes to effectively detect structural changes in G protein-coupled receptors (GPCRs), providing benefits like enhanced sensitivity to conformational changes and the ability to track fluorescence changes in response to different ligands.
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Article Synopsis
  • Secondary amyloidosis in humans is linked to the formation of hSAA fibrils in various tissues, challenging previous beliefs about hSAA's low amyloidogenic potential.
  • A new purification method for recombinant hSAA allows for the study of its aggregation behavior, revealing that it can undergo significant amyloid aggregation under physiological conditions.
  • The study found that the pH of the solution affects the type of amyloids formed, leading to different structural outcomes in protein aggregation.
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Background: The rat intestinal fatty acid-binding protein (I-FABP) is expressed in the small intestine and is involved in the absorption and transport of dietary fatty acids. It is used as a marker for intestinal injury and is associated with various gastrointestinal disorders. I-FABP has been studied extensively using conventional experimental and computational techniques.

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Morphological features and types of aggregated structures.

Prog Mol Biol Transl Sci

May 2024

Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Institute for Biological Instrumentation, Pushchino, Russia; Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United States. Electronic address:

Article Synopsis
  • Protein aggregation occurs when proteins fold incorrectly, leading to the formation of amyloid fibrils, which are linked to diseases like Alzheimer's and Parkinson's.
  • * Advances in imaging techniques, such as X-ray diffraction and cryo-electron microscopy, have improved our understanding of the complex structures of amyloid fibrils.
  • * This chapter summarizes recent research on protein aggregation, emphasizing the diverse structures of amyloids and their relevance to misfolding diseases.
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The hidden world of protein aggregation.

Prog Mol Biol Transl Sci

May 2024

Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Institute for Biological Instrumentation, Pushchino, Moscow, Russia; Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United States.

Though the book's journey into The Hidden World of Protein Aggregation has come to an end, the search for knowledge, the development of healthier lives, and the discovery of nature's mysteries continue, promising new horizons and discoveries yet to be discovered. The intricacies of protein misfolding and aggregation remain a mystery in cellular biology, despite advances made in unraveling them. In this chapter, we will summarize the specific conclusions from the previous chapters and explore the persistent obstacles and unanswered questions that motivate scientists to pursue exploration of protein misfolding and aggregation.

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Therapeutic approaches in proteinopathies.

Prog Mol Biol Transl Sci

May 2024

Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Institute for Biological Instrumentation, Pushchino, Moscow, Russia; Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United States. Electronic address:

A family of maladies known as amyloid disorders, proteinopathy, or amyloidosis, are characterized by the accumulation of abnormal protein aggregates containing cross-β-sheet amyloid fibrils in many organs and tissues. Often, proteins that have been improperly formed or folded make up these fibrils. Nowadays, most treatments for amyloid illness focus on managing symptoms rather than curing or preventing the underlying disease process.

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Liquid-liquid phase separation as triggering factor of fibril formation.

Prog Mol Biol Transl Sci

May 2024

Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Institute for Biological Instrumentation, Pushchino, Moscow, Russia; Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United States. Electronic address:

Liquid-liquid phase separation (LLPS) refers to the phenomenon, where a homogeneous solution spontaneously undergoes a transition into two or more immiscible phases. Through transient weak multivalent macromolecular interactions, a homogeneous solution can spontaneously separate into two phases: one rich in biomolecules and the other poor in biomolecules. Phase separation is believed to serve as the physicochemical foundation for the formation of membrane-less organelles (MLOs) and bio-molecular condensates within cells.

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Each big journey starts with a first step: Importance of oligomerization.

Prog Mol Biol Transl Sci

May 2024

Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Institute for Biological Instrumentation, Pushchino, Moscow, Russia; Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United Staes. Electronic address:

Protein oligomers, widely found in nature, have significant physiological and pathological functions. They are classified into three groups based on their function and toxicity. Significant advancements are being achieved in the development of functional oligomers, with a focus on various applications and their engineering.

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Protein aggregation: An overview.

Prog Mol Biol Transl Sci

May 2024

Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Institute for Biological Instrumentation, Pushchino, Moscow, Russia; Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United States. Electronic address:

In order for an ordered protein to perform its specific function, it must have a specific molecular structure. Information about this structure is encoded in the protein's amino acid sequence. The unique functional state is achieved as a result of a specific process, known as protein folding.

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Corrigendum to "Review: N1-methyl-pseudouridine (m1Ψ): Friend or foe of cancer?" [Int. J. Biol. Macromol. 267 (2024) 131427].

Int J Biol Macromol

June 2024

Biological Science Department, Faculty of Science, King Abdulaziz University, P.O. Box 80203, Jeddah 21589, Saudi Arabia; Therapeutic and Protective Proteins Laboratory, Protein Research Department, Genetic Engineering and Biotechnology Research Institute, City for Scientific Research and Technology Applications, New Borg EL-Arab, Alexandria 21934, Egypt.

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An imbalance between production and excretion of amyloid β peptide (Aβ) in the brain tissues of Alzheimer's disease (AD) patients leads to Aβ accumulation and the formation of noxious Aβ oligomers/plaques. A promising approach to AD prevention is the reduction of free Aβ levels by directed enhancement of Aβ binding to its natural depot, human serum albumin (HSA). We previously demonstrated the ability of specific low-molecular-weight ligands (LMWLs) in HSA to improve its affinity for Aβ.

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Review: N1-methyl-pseudouridine (m1Ψ): Friend or foe of cancer?

Int J Biol Macromol

May 2024

Biological Science Department, Faculty of Science, King Abdulaziz University, P.O. Box 80203, Jeddah 21589, Saudi Arabia; Therapeutic and Protective Proteins Laboratory, Protein Research Department, Genetic Engineering and Biotechnology Research Institute, City for Scientific Research and Technology Applications, New Borg EL-Arab, Alexandria 21934, Egypt. Electronic address:

Due to the health emergency created by SARS-CoV-2, the virus that causes the COVID-19 disease, the rapid implementation of a new vaccine technology was necessary. mRNA vaccines, being one of the cutting-edge new technologies, attracted significant interest and offered a lot of hope. The potential of these vaccines in preventing admission to hospitals and serious illness in people with comorbidities has recently been called into question due to the vaccines' rapidly waning immunity.

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Variation in base composition, structure-function relationships, and origins of structural repetition in bacterial rpsA gene.

Biosystems

April 2024

Institute of Protein Research, Russian Academy of Sciences, 142290, Pushchino, Moscow Region, Russia; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290, Pushchino, Moscow Region, Russia. Electronic address:

Protein domain repeats are known to arise due to tandem duplications of internal genes. However, the understanding of the underlying mechanisms of this process is incomplete. The goal of this work was to investigate the mechanism of occurrence of repeat expansion based on studying the sequences of 1324 rpsA genes of bacterial S1 ribosomal proteins containing different numbers of S1 structural domains.

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Recognition of granulocyte-macrophage colony-stimulating factor by specific S100 proteins.

Cell Calcium

May 2024

Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Institute for Biological Instrumentation, Institutskaya str., 7, Pushchino, Moscow Region 142290, Russia. Electronic address:

Granulocyte-macrophage colony-stimulating factor (GM-CSF) is a pleiotropic myelopoietic growth factor and proinflammatory cytokine, clinically used for multiple indications and serving as a promising target for treatment of many disorders, including cancer, multiple sclerosis, rheumatoid arthritis, psoriasis, asthma, COVID-19. We have previously shown that dimeric Ca-bound forms of S100A6 and S100P proteins, members of the multifunctional S100 protein family, are specific to GM-CSF. To probe selectivity of these interactions, the affinity of recombinant human GM-CSF to dimeric Ca-loaded forms of 18 recombinant human S100 proteins was studied by surface plasmon resonance spectroscopy.

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Myricetin is a flavonol with high antioxidant properties. In this research, the fluorescence emission of myricetin powder and its solutions in different solvents were measured and analyzed by comparing with the results of calculations. Comparison of the calculated and measured characteristic wavelengths allowed the identification of all the spectral features in the fluorescence spectra of myricetin powder and solutions with different concentrations.

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Reexamining the diverse functions of arginine in biochemistry.

Biochem Biophys Res Commun

April 2024

Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Institute for Biological Instrumentation, Institutskaya Str., 7, Pushchino, Moscow Region, 142290, Russia; Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, 33612, USA. Electronic address:

Arginine in a free-state and as part of peptides and proteins shows distinct tendency to form clusters. In free-form, it has been found useful in cryoprotection, as a drug excipient for both solid and liquid formulations, as an aggregation suppressor, and an eluent in protein chromatography. In many cases, the mechanisms by which arginine acts in all these applications is either debatable or at least continues to attract interest.

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