Full Text Journal Articles by
Author Yury O Chernoff

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Development of molecular tools for diagnosis of Alzheimer's disease that are based on detection of amyloidogenic proteins.

Konstantin Y Kulichikhin, Sergei A Fedotov, Maria S Rubel, Natalia M Zalutskaya, Anastasia E Zobnina, Oksana A Malikova, Nikolay G Neznanov, Yury O Chernoff, Aleksandr A Rubel,

Alzheimer's disease (AD) is the most common form of dementia that usually occurs among older people. AD results from neuronal degeneration that leads to the cognitive impairment and death. AD is incurable, typically develops over the course of many years and is accompanied by a loss of functional autonomy, making ... Read more >>

Prion (Prion)
[2021, 15(1):56-69]

Cited: 1 time

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Modeling Amyloid Aggregation Kinetics: A Case Study with Sup35NM.

Aditi Sharma, Matthew A McDonald, Harrison B Rose, Yury O Chernoff, Sven H Behrens, Andreas S Bommarius,

Understanding the aggregation mechanism of amyloid proteins, such as Sup35NM, is essential to understanding amyloid diseases. Significant recent work has focused on using the fluorescence of thioflavin T (ThT), which undergoes a red shift when bound to amyloid aggregates, to monitor amyloid fibril formation. In the present study, the progression ... Read more >>

J Phys Chem B (The journal of physical chemistry. B)
[2021, 125(19):4955-4963]

Cited: 0 times

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Design and synthesis of novel tacrine-indole hybrids as potential multitarget-directed ligands for the treatment of Alzheimer's disease.

Slavka Hamulakova, Zuzana Kudlickova, Ladislav Janovec, Roman Mezencev, Zachery J Deckner, Yury O Chernoff, Jana Janockova, Veronika Ihnatova, Petr Bzonek, Nikola Novakova, Vendula Hepnarova, Martina Hrabinova, Daniel Jun, Jan Korabecny, Ondrej Soukup, Kamil Kuca,

The authors report on the synthesis and biological evaluation of new compounds whose structure combines tacrine and indole moieties. Tacrine-indole heterodimers were designed to inhibit cholinesterases and β-amyloid formation, and to cross the blood-brain barrier. The most potent new acetylcholinesterase inhibitors were compounds <b>3c</b> and <b>4d</b> (IC<sub>50</sub> = 25 and 39 nM, respectively). ... Read more >>

Future Med Chem (Future medicinal chemistry)
[2021, 13(9):785-804]

Cited: 0 times

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Regulation of the endocytosis and prion-chaperoning machineries by yeast E3 ubiquitin ligase Rsp5 as revealed by orthogonal ubiquitin transfer.

Yiyang Wang, Shuai Fang, Geng Chen, Rakhee Ganti, Tatiana A Chernova, Li Zhou, Duc Duong, Hiroaki Kiyokawa, Ming Li, Bo Zhao, Natalia Shcherbik, Yury O Chernoff, Jun Yin,

Attachment of the ubiquitin (UB) peptide to proteins via the E1-E2-E3 enzymatic machinery regulates diverse biological pathways, yet identification of the substrates of E3 UB ligases remains a challenge. We overcame this challenge by constructing an "orthogonal UB transfer" (OUT) cascade with yeast E3 Rsp5 to enable the exclusive delivery of ... Read more >>

Cell Chem Biol (Cell chemical biology)
[2021, 28(9):1283-1297.e8]

Cited: 1 time

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Aggregation and Prion-Inducing Properties of the G-Protein Gamma Subunit Ste18 are Regulated by Membrane Association.

Tatiana A Chernova, Zhen Yang, Tatiana S Karpova, John R Shanks, Natalia Shcherbik, Keith D Wilkinson, Yury O Chernoff,

Yeast prions and mnemons are respectively transmissible and non-transmissible self-perpetuating protein assemblies, frequently based on cross-β ordered detergent-resistant aggregates (amyloids). Prions cause devastating diseases in mammals and control heritable traits in yeast. It was shown that the de novo formation of the prion form [<i>PSI</i><sup>+</sup>] of yeast release factor Sup35 ... Read more >>

Int J Mol Sci (International journal of molecular sciences)
[2020, 21(14):]

Cited: 1 time

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Functional Mammalian Amyloids and Amyloid-Like Proteins.

Maria S Rubel, Sergey A Fedotov, Anastasia V Grizel, Julia V Sopova, Oksana A Malikova, Yury O Chernoff, Aleksandr A Rubel,

Amyloids are highly ordered fibrous cross-β protein aggregates that are notorious primarily because of association with a variety of incurable human and animal diseases (termed amyloidoses), including Alzheimer's disease (AD), Parkinson's disease (PD), type 2 diabetes (T2D), and prion diseases. Some amyloid-associated diseases, in particular T2D and AD, are widespread ... Read more >>

Life (Basel) (Life (Basel, Switzerland))
[2020, 10(9):]

Cited: 5 times

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Protein Misfolding during Pregnancy: New Approaches to Preeclampsia Diagnostics.

Elizaveta M Gerasimova, Sergey A Fedotov, Daniel V Kachkin, Elena S Vashukova, Andrey S Glotov, Yury O Chernoff, Aleksandr A Rubel,

Preeclampsia (PE) is a multisystem heterogeneous complication of pregnancy remaining a leading cause of maternal and perinatal morbidity and mortality over the world. PE has a large spectrum of clinical features and symptoms, which make diagnosis challenging. Despite a long period of studying, PE etiology is still unclear and there ... Read more >>

Int J Mol Sci (International journal of molecular sciences)
[2019, 20(24):]

Cited: 6 times

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Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery.

Tatiana A Chernova, Yury O Chernoff, Keith D Wilkinson,

Amyloids are self-perpetuating protein aggregates causing neurodegenerative diseases in mammals. Prions are transmissible protein isoforms (usually of amyloid nature). Prion features were recently reported for various proteins involved in amyloid and neural inclusion disorders. Heritable yeast prions share molecular properties (and in the case of polyglutamines, amino acid composition) with ... Read more >>

Molecules (Molecules (Basel, Switzerland))
[2019, 24(18):]

Cited: 6 times

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Proteolysis suppresses spontaneous prion generation in yeast.

Atsushi Okamoto, Nao Hosoda, Anri Tanaka, Gary P Newnam, Yury O Chernoff, Shin-Ichi Hoshino,

Prions are infectious proteins that cause fatal neurodegenerative disorders including Creutzfeldt-Jakob and bovine spongiform encephalopathy (mad cow) diseases. The yeast [<i>PSI</i><sup>+</sup>] prion is formed by the translation-termination factor Sup35, is the best-studied prion, and provides a useful model system for studying such diseases. However, despite recent progress in the understanding ... Read more >>

J Biol Chem (The Journal of biological chemistry)
[2017, 292(49):20113-20124]

Cited: 7 times

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Mammalian amyloidogenic proteins promote prion nucleation in yeast.

Pavithra Chandramowlishwaran, Meng Sun, Kristin L Casey, Andrey V Romanyuk, Anastasiya V Grizel, Julia V Sopova, Aleksandr A Rubel, Carmen Nussbaum-Krammer, Ina M Vorberg, Yury O Chernoff,

Fibrous cross-β aggregates (amyloids) and their transmissible forms (prions) cause diseases in mammals (including humans) and control heritable traits in yeast. Initial nucleation of a yeast prion by transiently overproduced prion-forming protein or its (typically, QN-rich) prion domain is efficient only in the presence of another aggregated (in most cases, ... Read more >>

J Biol Chem (The Journal of biological chemistry)
[2018, 293(9):3436-3450]

Cited: 6 times

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Differential effects of chaperones on yeast prions: CURrent view.

Andrew G Matveenko, Yury A Barbitoff, Lina Manuela Jay-Garcia, Yury O Chernoff, Galina A Zhouravleva,

Endogenous yeast amyloids that control heritable traits and are frequently used as models for human amyloid diseases are termed yeast prions. Yeast prions, including the best studied ones ([PSI <sup>+</sup>] and [URE3]), propagate via intimate interactions with molecular chaperones. Different yeast prions exhibit differential responses to changes in levels, functionality ... Read more >>

Curr Genet (Current genetics)
[2018, 64(2):317-325]

Cited: 12 times

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To CURe or not to CURe? Differential effects of the chaperone sorting factor Cur1 on yeast prions are mediated by the chaperone Sis1.

Yury A Barbitoff, Andrew G Matveenko, Svetlana E Moskalenko, Olga M Zemlyanko, Gary P Newnam, Ayesha Patel, Tatiana A Chernova, Yury O Chernoff, Galina A Zhouravleva,

Yeast self-perpetuating protein aggregates (prions) provide a convenient model for studying various components of the cellular protein quality control system. Molecular chaperones and chaperone-sorting factors, such as yeast Cur1 protein, play key role in proteostasis via tight control of partitioning and recycling of misfolded proteins. In this study, we show ... Read more >>

Mol Microbiol (Molecular microbiology)
[2017, 105(2):242-257]

Cited: 12 times

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Prion-based memory of heat stress in yeast.

Tatiana A Chernova, Yury O Chernoff, Keith D Wilkinson,

Amyloids and amyloid-based prions are self-perpetuating protein aggregates which can spread by converting a normal protein of the same sequence into a prion form. They are associated with diseases in humans and mammals, and control heritable traits in yeast and other fungi. Some amyloids are implicated in biologically beneficial processes. ... Read more >>

Prion (Prion)
[2017, 11(3):151-161]

Cited: 9 times

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In memory of Susan Lindquist (1949-2016).

Yury O Chernoff,

Prion (Prion)
[2017, 11(1):1-3]

Cited: 1 time

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Yeast Short-Lived Actin-Associated Protein Forms a Metastable Prion in Response to Thermal Stress.

Tatiana A Chernova, Denis A Kiktev, Andrey V Romanyuk, John R Shanks, Oskar Laur, Moiez Ali, Abheek Ghosh, Dami Kim, Zhen Yang, Maggie Mang, Yury O Chernoff, Keith D Wilkinson,

Self-perpetuating ordered protein aggregates (amyloids and prions) are associated with a variety of neurodegenerative disorders. Although environmental agents have been linked to certain amyloid diseases, the molecular basis of their action remains unclear. We have employed endogenous yeast prions as a model system to study environmental control of amyloid formation. ... Read more >>

Cell Rep (Cell reports)
[2017, 18(3):751-761]

Cited: 24 times

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Prions, Chaperones, and Proteostasis in Yeast.

Tatiana A Chernova, Keith D Wilkinson, Yury O Chernoff,

Prions are alternatively folded, self-perpetuating protein isoforms involved in a variety of biological and pathological processes. Yeast prions are protein-based heritable elements that serve as an excellent experimental system for studying prion biology. The propagation of yeast prions is controlled by the same Hsp104/70/40 chaperone machinery that is involved in ... Read more >>

Cold Spring Harb Perspect Biol (Cold Spring Harbor perspectives in biology)
[2017, 9(2):]

Cited: 31 times

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Distinct types of translation termination generate substrates for ribosome-associated quality control.

Natalia Shcherbik, Tatiana A Chernova, Yury O Chernoff, Dimitri G Pestov,

Cotranslational degradation of polypeptide nascent chains plays a critical role in quality control of protein synthesis and the rescue of stalled ribosomes. In eukaryotes, ribosome stalling triggers release of 60S subunits with attached nascent polypeptides, which undergo ubiquitination by the E3 ligase Ltn1 and proteasomal degradation facilitated by the ATPase ... Read more >>

Nucleic Acids Res (Nucleic acids research)
[2016, 44(14):6840-6852]

Cited: 16 times

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Strain conformation controls the specificity of cross-species prion transmission in the yeast model.

Anastasia V Grizel, Aleksandr A Rubel, Yury O Chernoff,

Transmissible self-assembled fibrous cross-β polymer infectious proteins (prions) cause neurodegenerative diseases in mammals and control non-Mendelian heritable traits in yeast. Cross-species prion transmission is frequently impaired, due to sequence differences in prion-forming proteins. Recent studies of prion species barrier on the model of closely related yeast species show that colocalization ... Read more >>

Prion (Prion)
[2016, 10(4):269-282]

Cited: 1 time

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Dual role of ribosome-associated chaperones in prion formation and propagation.

Yury O Chernoff, Denis A Kiktev,

Chaperones of the diverse ubiquitous Hsp70 family are involved in the regulation of ordered self-perpetuating protein aggregates (amyloids and prions), implicated in both devastating diseases and protein-based inheritance. Yeast ribosome-associated chaperone complex (RAC), composed of the Hsp40 protein Zuo1 and non-canonical Hsp70 protein Ssz1, mediates association of the Hsp70 chaperone ... Read more >>

Curr Genet (Current genetics)
[2016, 62(4):677-685]

Cited: 18 times

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Contributions of the Prion Protein Sequence, Strain, and Environment to the Species Barrier.

Aditi Sharma, Kathryn L Bruce, Buxin Chen, Stefka Gyoneva, Sven H Behrens, Andreas S Bommarius, Yury O Chernoff,

Amyloid propagation requires high levels of sequence specificity so that only molecules with very high sequence identity can form cross-β-sheet structures of sufficient stringency for incorporation into the amyloid fibril. This sequence specificity presents a barrier to the transmission of prions between two species with divergent sequences, termed a species ... Read more >>

J Biol Chem (The Journal of biological chemistry)
[2016, 291(3):1277-1288]

Cited: 14 times

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The call of the unknown: The story of [PSI(+)].

Yury O Chernoff,

Prion (Prion)
[2015, 9(5):315-317]

Cited: 1 time

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Feedback control of prion formation and propagation by the ribosome-associated chaperone complex.

Denis A Kiktev, Mikhail M Melomed, Caroline D Lu, Gary P Newnam, Yury O Chernoff,

Cross-beta fibrous protein aggregates (amyloids and amyloid-based prions) are found in mammals (including humans) and fungi (including yeast), and are associated with both diseases and heritable traits. The Hsp104/70/40 chaperone machinery controls propagation of yeast prions. The Hsp70 chaperones Ssa and Ssb show opposite effects on [PSI(+)], a prion form ... Read more >>

Mol Microbiol (Molecular microbiology)
[2015, 96(3):621-632]

Cited: 23 times

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Physiological and environmental control of yeast prions.

Tatiana A Chernova, Keith D Wilkinson, Yury O Chernoff,

Prions are self-perpetuating protein isoforms that cause fatal and incurable neurodegenerative disease in mammals. Recent evidence indicates that a majority of human proteins involved in amyloid and neural inclusion disorders possess at least some prion properties. In lower eukaryotes, such as yeast, prions act as epigenetic elements, which increase phenotypic ... Read more >>

FEMS Microbiol Rev (FEMS microbiology reviews)
[2014, 38(2):326-344]

Cited: 38 times

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Regulation of chaperone effects on a yeast prion by cochaperone Sgt2.

Denis A Kiktev, Jesse C Patterson, Susanne Müller, Bhawana Bariar, Tao Pan, Yury O Chernoff,

Yeast prions, based on self-seeded highly ordered fibrous aggregates (amyloids), serve as a model for human amyloid diseases. Propagation of yeast prions depends on the balance between chaperones of the Hsp100 and Hsp70 families. The yeast prion [PSI(+)] can be eliminated by an excess of the chaperone Hsp104. This effect ... Read more >>

Mol Cell Biol (Molecular and cellular biology)
[2012, 32(24):4960-4970]

Cited: 43 times

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A special focus issue on the materials of Prion 2011 meeting in Montreal, Canada.

Neil R Cashman, Yury O Chernoff,

Prion (Prion)
[2012, 6(2):95-96]

Cited: 0 times

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