16 results on '"Petyuk, V. A."'
Search Results
2. Proteogenomic Characterization of Difficult-to-Treat Breast Cancer with Tumor Cells Enriched through Laser Microdissection
- Author
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Surgery (SUR), SOM, Kumar-P., Lin-X., Liu-T., Sturtz-L., Gritsenko-M., Petyuk-V., Sagendorf-T., Deyarmin-B., Lui-J., Kumar-AP., Wang-G., McDermott-J., Shukla-A., Moore-R., Monroe-M., Webb-Robertson-BJ., Hooke-JA., Fantacone-Campbell-L., Mostoller-B., Kvecher-L., Kane-J., Melley-J., Somiari-S., Soon Shiong-P., Smith-R., Mural-R., Surgery (SUR), SOM, Kumar-P., and Lin-X., Liu-T., Sturtz-L., Gritsenko-M., Petyuk-V., Sagendorf-T., Deyarmin-B., Lui-J., Kumar-AP., Wang-G., McDermott-J., Shukla-A., Moore-R., Monroe-M., Webb-Robertson-BJ., Hooke-JA., Fantacone-Campbell-L., Mostoller-B., Kvecher-L., Kane-J., Melley-J., Somiari-S., Soon Shiong-P., Smith-R., Mural-R.
- Abstract
RITM0045863, Four well-defined subtypes of Breast Cancer (BC) based on PAM50 transcripts: basallike (Basal) , Her2-enriched (Her2), Luminal B (LumB), and Luminal A (LumA). ? There is still considerable variation in the clinical outcomes of patients with non- LumA tumors, which can be classified as difficult-to-treat breast cancers (DTBC) ? Previous proteogenomic work (TCGA, CPTAC etc.) analyzed BCs from the general population with bulk tissue processing. ? Herein, we performed a proteogenomic characterization of DTBC tumors in reference to LumA tumors, from patients with long follow-up, and using Laser Microdissection (LMD) processing to enrich tumor cells.
- Published
- 2023
3. Kinetic Parameters of Cleavage of CpA and UpA Sequences in an Oligoribonucleotide by Compounds Functionally Mimicking Ribonuclease A
- Author
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Beloglazova, N. G., Mironova, N. L., Konevets, D. A., Petyuk, V. A., Sil'nikov, V. N., Vlasov, V. V., and Zenkova, M. A.
- Published
- 2002
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4. Hybridization of antisense oligonucleotides with yeast tRNAPhe: factors determining the efficiency of interaction
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Serikov, R. N., Petyuk, V. A., Vlassov, V. V., and Zenkova, M. A.
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- 2002
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5. Mechanism of oligonucleotide hybridization with the 3′-terminal region of the yeast tRNAPhe
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Petyuk, V. A., Giege, R., Vlassov, V. V., and Zenkova, M. A.
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- 2000
- Full Text
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6. Identification of Hip BMD Loss and Fracture Risk Markers Through Population-Based Serum Proteomics
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Nielson, CM, Wiedrick, J, Shen, J, Jacobs, J, Baker, ES, Baraff, A, Piehowski, P, Lee, CG, Baratt, A, Petyuk, V, McWeeney, S, Lim, JY, Bauer, DC, Lane, NE, Cawthon, PM, Smith, RD, Lapidus, J, and Orwoll, ES
- Subjects
Osteoporotic Fractures in Men (MrOS) Study Research Group ,Proteomics ,Aged, 80 and over ,Male ,Medical And Health Sciences ,Hip ,Proteome ,Hip Fractures ,Biological Sciences ,OSTEOPOROSIS ,Anatomy & Morphology ,BIOCHEMICAL MARKERS OF BONE TURNOVER ,Engineering ,Bone Density ,Humans ,GENERAL POPULATION STUDIES ,Peptides ,Biomarkers ,Aged - Abstract
© 2017 American Society for Bone and Mineral Research Serum proteomics analysis may lead to the discovery of novel osteoporosis biomarkers. The Osteoporotic Fractures in Men (MrOS) study comprises men ≥65 years old in the US who have had repeated BMD measures and have been followed for incident fracture. High-throughput quantitative proteomic analysis was performed on baseline fasting serum samples from non-Hispanic white men using a multidimensional approach coupling liquid chromatography, ion-mobility separation, and mass spectrometry (LC-IMS-MS). We followed the participants for a mean of 4.6 years for changes in femoral neck bone mineral density (BMD) and for incident hip fracture. Change in BMD was determined from mixed effects regression models taking age and weight into account. Participants were categorized into three groups: BMD maintenance (no decline; estimated change ≥0 g/cm2, n = 453); expected loss (estimated change 0 to 1 SD below the estimated mean change, –0.034 g/cm2for femoral neck, n = 1184); and accelerated loss (estimated change ≥1 SD below mean change, n = 237). Differential abundance values of 3946 peptides were summarized by meta-analysis to determine differential abundance of each of 339 corresponding proteins for accelerated BMD loss versus maintenance. Using this meta-analytic standardized fold change at cutoffs of ≥1.1 or ≤0.9 (p < 0.10), 20 proteins were associated with accelerated BMD loss. Associations of those 20 proteins with incident hip fracture were tested using Cox proportional hazards models with age and BMI adjustment in 2473 men. Five proteins were associated with incident hip fracture (HR between 1.29 and 1.41 per SD increase in estimated protein abundance). Some proteins have been previously associated with fracture risk (eg, CD14 and SHBG), whereas others have roles in cellular senescence and aging (B2MG and TIMP1) and complement activation and innate immunity (CO7, CO9, CFAD). These findings may inform development of biomarkers for future research in bone biology and fracture prediction. © 2017 American Society for Bone and Mineral Research.
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- 2017
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7. Chapter 14: R for Proteomics
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University of Cambridge, Breckels, L.M., Gibb, S., Petyuk, V., Gatto, Laurent, University of Cambridge, Breckels, L.M., Gibb, S., Petyuk, V., and Gatto, Laurent
- Published
- 2017
8. Role of CTGF in Sensitivity to Hyperthermia in Ovarian and Uterine Cancers
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Hatakeyama, H., Wu, S. Y., Lyons, Y. A., Pradeep, S., Wang, W., Huang, Q., Court, K. A., Liu, T., Nie, S., Rodriguez-Aguayo, C., Shen, F., Huang, Y., Hisamatsu, T., Mitamura, T., Jennings, N., Shim, J., Dorniak, P. L., Mangala, L. S., Petrillo, Marco, Petyuk, V. A., Schepmoes, A. A., Shukla, A. K., Torres-Lugo, M., Lee, J. -S., Rodland, K. D., Fagotti, Anna, Lopez-Berestein, G., Li, C., Sood, A. K., Petrillo M., Fagotti A. (ORCID:0000-0001-5579-335X), Hatakeyama, H., Wu, S. Y., Lyons, Y. A., Pradeep, S., Wang, W., Huang, Q., Court, K. A., Liu, T., Nie, S., Rodriguez-Aguayo, C., Shen, F., Huang, Y., Hisamatsu, T., Mitamura, T., Jennings, N., Shim, J., Dorniak, P. L., Mangala, L. S., Petrillo, Marco, Petyuk, V. A., Schepmoes, A. A., Shukla, A. K., Torres-Lugo, M., Lee, J. -S., Rodland, K. D., Fagotti, Anna, Lopez-Berestein, G., Li, C., Sood, A. K., Petrillo M., and Fagotti A. (ORCID:0000-0001-5579-335X)
- Abstract
Even though hyperthermia is a promising treatment for cancer, the relationship between specific temperatures and clinical benefits and predictors of sensitivity of cancer to hyperthermia is poorly understood. Ovarian and uterine tumors have diverse hyperthermia sensitivities. Integrative analyses of the specific gene signatures and the differences in response to hyperthermia between hyperthermia-sensitive and -resistant cancer cells identified CTGF as a key regulator of sensitivity. CTGF silencing sensitized resistant cells to hyperthermia. CTGF small interfering RNA (siRNA) treatment also sensitized resistant cancers to localized hyperthermia induced by copper sulfide nanoparticles and near-infrared laser in orthotopic ovarian cancer models. CTGF silencing aggravated energy stress induced by hyperthermia and enhanced apoptosis of hyperthermia-resistant cancers.
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- 2016
9. Mechanism of Antisense Oligonucleotide Interaction with Natural RNAs
- Author
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Serikov, R., primary, Petyuk, V., additional, Vorobijev, Yu., additional, Koval, V., additional, Fedorova, O., additional, Vlassov, V., additional, and Zenkova, M., additional
- Published
- 2011
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10. Invasion of Strongly Binding Oligonucleotides into tRNA Structure
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Petyuk, V., primary, Serikov, R., additional, Tolstikov, V., additional, Potapov, V., additional, Giege, R., additional, Zenkova, M., additional, and Vlassov, V., additional
- Published
- 2000
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11. Interaction of Complementary Oligonucleotides with the 3′-End of Yeast tRNAPHE
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Petyuk, V., primary, Zenkova, M., additional, Giege, R., additional, and Vlassov, V., additional
- Published
- 1999
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12. Mechanism of oligonucleotide hybridization with the 3′-terminal region of the yeast tRNAPhe.
- Author
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Petyuk, V., Giege, R., Vlassov, V., and Zenkova, M.
- Abstract
Interaction of yeast phenylalanine tRNA with oligonucleotides complementary to its 3′-terminal nucleotide sequence was thoroughly studied. Using the gel retardation technique, thermodynamic and kinetic parameters of the tRNA complexation in physiological conditions were determined. Analysis of dependences of the complex formation on the oligonucleotide concentration and incubation time showed that this process proceeds in two stages. At the first stage, a metastable complex of the oligonucleotide with the open, single-stranded sequence ACCA at the 3′ end of tRNA rapidly forms. The second stage involves a slow intramolecular rearrangement of the resulting metastable complex into a full-sized heteroduplex accompanied by the tRNA
Phe unfolding. The data gained suggest that the RNA unfolding stage is limiting in the interaction of oligonucleotides with natural RNAs. Principles of selection of optimal hybridization probes and antisense oligonucleotides are discussed. [ABSTRACT FROM AUTHOR]- Published
- 2000
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13. Hybridization of antisense oligonucleotides with the 3' part of tRNA^P^h^e
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Petyuk, V. A., Zenkova, M. A., Giege, R., and Vlassov, V. V.
- Published
- 1999
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14. Time-Resolved Proteome, Metabolome And Lipidome Profiling Of Normal Lung Development
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Moghieb, A. M., Clair, G., Kyle, J., Young-Mo Kim, Zink, E., Petyuk, V. A., Corley, R., and Ansong, C.
15. Proteogenomic and metabolomic characterization of human glioblastoma
- Author
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Cristina E. Tognon, Larisa Polonskaya, Tara Skelly, Shuang Cai, Francesmary Modugno, Larissa Rossell, Nancy Roche, Chen Huang, Jessika Baral, Fulvio D'Angelo, Wen-Wei Liang, Chia-Feng Tsai, Sneha P. Couvillion, Karin D. Rodland, Jun Zhu, Liang-Bo Wang, Paul D. Piehowski, Antonio Colaprico, Anupriya Agarwal, Matthew A. Wyczalkowski, Umut Ozbek, Francesca Petralia, Alexis Demopoulos, William W. Maggio, Lin Chen, Katherine A. Hoadley, Richard D. Smith, Sandra Cottingham, John McGee, Marcin J. Domagalski, Houxiang Zhu, Emek Demir, Rebecca I. Montgomery, Jamie Moon, Rashna Madan, George D. Wilson, Luciano Garofano, Ewa P. Malc, Chelsea J. Newton, Steven A. Carr, Chandan Kumar-Sinha, Donghui Tan, Christopher R. Kinsinger, Oxana Paklina, Weiqing Wan, Stephanie De Young, Sandra Cerda, Shankha Satpathy, Wojciech Kaspera, Linda Hannick, Gad Getz, Runyu Hong, Shuangjia Lu, Ziad Hanhan, Daniel C. Rohrer, Annette Marrero-Oliveras, Wojciech Szopa, Yuxing Liao, Amanda G. Paulovich, Jiayi Ji, Denis A. Golbin, Tara Hiltke, Weiva Sieh, Piotr A. Mieczkowski, Matthew E. Monroe, Gilbert S. Omenn, Jill S. Barnholtz-Sloan, Azra Krek, Bing Zhang, Brittany Henderson, Peter B. McGarvey, Ratna R. Thangudu, Maciej Wiznerowicz, Saravana M. Dhanasekaran, Alex Webster, Kai Li, Karna Robinson, Nan Ji, Karl K. Weitz, Simina M. Boca, Xiaoyu Song, Anna Calinawan, Adam C. Resnick, Brian J. Druker, Dana R. Valley, David J. Clark, Tao Liu, Eric J. Jaehnig, Alicia Francis, Michele Ceccarelli, Rui Zhao, Dmitry Rykunov, Boris Reva, Elizabeth R. Duffy, Antonio Iavarone, Dave Tabor, Joshua F. McMichael, Daniel Cui Zhou, Maureen Dyer, Kimberly Elburn, Scott D. Jewell, Negin Vatanian, Shirley Tsang, Seungyeul Yoo, Alexander R. Pico, Grace Zhao, Kent J. Bloodsworth, Chet Birger, Jena Lilly, Eunkyung An, Jeffrey R. Whiteaker, Albert H. Kim, Yige Wu, Karen A. Ketchum, Felipe D. Leprevost, Alcida Karz, Uma Borate, Nathan Edwards, Uma Velvulou, Melissa Borucki, Vasileios Stathias, Sanford P. Markey, Corbin D. Jones, Ronald J. Moore, MacIntosh Cornwell, Karsten Krug, Michael J. Birrer, James Suh, Tomasz Czernicki, Jason E. McDermott, Emily S. Boja, Pei Wang, Nina Martinez, Wenke Liu, Yan Shi, Lili Blumenberg, Emily Kawaler, Jeffrey W. Tyner, Feng Chen, Jakub Stawicki, Ki Sung Um, Arul M. Chinnaiyan, Robert Zelt, Jacob J. Day, Zhen Zhang, Caleb M. Lindgren, Li Ding, Nikolay Gabrovski, Hongwei Liu, Jonathan T. Lei, Alla Karpova, Ramani B. Kothadia, Sailaja Mareedu, Mitual Amin, Hannah Boekweg, Jennifer E. Kyle, Sara R. Savage, Brian R. Rood, Yuriy Zakhartsev, Matthew L. Anderson, Alyssa Charamut, Wagma Caravan, Shakti Ramkissoon, Junmei Wang, Song Cao, Samuel H. Payne, Rosalie K. Chu, Rajiv Dhir, David W. Andrews, Galen Hostetter, Liqun Qi, Zhiao Shi, Milan G. Chheda, Robert Edwards, Hui Zhang, Weiping Ma, Jennifer M. Eschbacher, Stacey Gabriel, Jan Lubinski, Lijun Yao, Erika M. Zink, Kelly L. Stratton, William Bocik, Mathangi Thiagarajan, Shilpi Singh, Michael A. Gillette, Lisa M. Bramer, Thomas L. Bauer, Michael Vernon, Henry Rodriguez, Dimitris G. Placantonakis, Eric E. Schadt, Alexey I. Nesvizhskii, Vladislav A. Petyuk, Ana I. Robles, Yvonne Shutack, Anna Malovannaya, Stephen E. Stein, Xi Chen, Lyndon Kim, Yize Li, Shannon Richey, Stephan C. Schürer, Barbara Hindenach, Matthew J. Ellis, Yongchao Dou, David Fenyö, Amy M. Perou, Olga Potapova, Shrabanti Chowdhury, Andrew K. Godwin, Marcin Cieślik, Michael C. Wendl, Marina A. Gritsenko, Pietro Pugliese, Elie Traer, Simona Migliozzi, D. R. Mani, Houston Culpepper, Gregory J. Riggins, Xiaolu Yang, Mehdi Mesri, David Chesla, Lindsey K. Olsen, Lori J. Sokoll, Suhas Vasaikar, Liwei Zhang, Meghan C. Burke, Kelly V. Ruggles, Qing Kay Li, Daniel W. Chan, Bo Wen, Nicollette Maunganidze, Darlene Tansil, Joseph H. Rothstein, Barbara Pruetz, Pushpa Hariharan, Wang, L. -B., Karpova, A., Gritsenko, M. A., Kyle, J. E., Cao, S., Li, Y., Rykunov, D., Colaprico, A., Rothstein, J. H., Hong, R., Stathias, V., Cornwell, M., Petralia, F., Wu, Y., Reva, B., Krug, K., Pugliese, P., Kawaler, E., Olsen, L. K., Liang, W. -W., Song, X., Dou, Y., Wendl, M. C., Caravan, W., Liu, W., Cui Zhou, D., Ji, J., Tsai, C. -F., Petyuk, V. A., Moon, J., Ma, W., Chu, R. K., Weitz, K. K., Moore, R. J., Monroe, M. E., Zhao, R., Yang, X., Yoo, S., Krek, A., Demopoulos, A., Zhu, H., Wyczalkowski, M. A., Mcmichael, J. F., Henderson, B. L., Lindgren, C. M., Boekweg, H., Lu, S., Baral, J., Yao, L., Stratton, K. G., Bramer, L. M., Zink, E., Couvillion, S. P., Bloodsworth, K. J., Satpathy, S., Sieh, W., Boca, S. M., Schurer, S., Chen, F., Wiznerowicz, M., Ketchum, K. A., Boja, E. S., Kinsinger, C. R., Robles, A. I., Hiltke, T., Thiagarajan, M., Nesvizhskii, A. I., Zhang, B., Mani, D. R., Ceccarelli, M., Chen, X. S., Cottingham, S. L., Li, Q. K., Kim, A. H., Fenyo, D., Ruggles, K. V., Rodriguez, H., Mesri, M., Payne, S. H., Resnick, A. C., Wang, P., Smith, R. D., Iavarone, A., Chheda, M. G., Barnholtz-Sloan, J. S., Rodland, K. D., Liu, T., Ding, L., Agarwal, A., Amin, M., An, E., Anderson, M. L., Andrews, D. W., Bauer, T., Birger, C., Birrer, M. J., Blumenberg, L., Bocik, W. E., Borate, U., Borucki, M., Burke, M. C., Cai, S., Calinawan, A. P., Carr, S. A., Cerda, S., Chan, D. W., Charamut, A., Chen, L. S., Chesla, D., Chinnaiyan, A. M., Chowdhury, S., Cieslik, M. P., Clark, D. J., Culpepper, H., Czernicki, T., D'Angelo, F., Day, J., De Young, S., Demir, E., Dhanasekaran, S. M., Dhir, R., Domagalski, M. J., Druker, B., Duffy, E., Dyer, M., Edwards, N. J., Edwards, R., Elburn, K., Ellis, M. J., Eschbacher, J., Francis, A., Gabriel, S., Gabrovski, N., Garofano, L., Getz, G., Gillette, M. A., Godwin, A. K., Golbin, D., Hanhan, Z., Hannick, L. I., Hariharan, P., Hindenach, B., Hoadley, K. A., Hostetter, G., Huang, C., Jaehnig, E., Jewell, S. D., Ji, N., Jones, C. D., Karz, A., Kaspera, W., Kim, L., Kothadia, R. B., Kumar-Sinha, C., Lei, J., Leprevost, F. D., Li, K., Liao, Y., Lilly, J., Liu, H., Lubinski, J., Madan, R., Maggio, W., Malc, E., Malovannaya, A., Mareedu, S., Markey, S. P., Marrero-Oliveras, A., Martinez, N., Maunganidze, N., Mcdermott, J. E., Mcgarvey, P. B., Mcgee, J., Mieczkowski, P., Migliozzi, S., Modugno, F., Montgomery, R., Newton, C. J., Omenn, G. S., Ozbek, U., Paklina, O. V., Paulovich, A. G., Perou, A. M., Pico, A. R., Piehowski, P. D., Placantonakis, D. G., Polonskaya, L., Potapova, O., Pruetz, B., Qi, L., Ramkissoon, S., Resnick, A., Richey, S., Riggins, G., Robinson, K., Roche, N., Rohrer, D. C., Rood, B. R., Rossell, L., Savage, S. R., Schadt, E. E., Shi, Y., Shi, Z., Shutack, Y., Singh, S., Skelly, T., Sokoll, L. J., Stawicki, J., Stein, S. E., Suh, J., Szopa, W., Tabor, D., Tan, D., Tansil, D., Thangudu, R. R., Tognon, C., Traer, E., Tsang, S., Tyner, J., Um, K. S., Valley, D. R., Vasaikar, S., Vatanian, N., Velvulou, U., Vernon, M., Wan, W., Wang, J., Webster, A., Wen, B., Whiteaker, J. R., Wilson, G. D., Zakhartsev, Y., Zelt, R., Zhang, H., Zhang, L., Zhang, Z., Zhao, G., and Zhu, J.
- Subjects
Proteomics ,0301 basic medicine ,Cancer Research ,CPTAC ,Histone H2B acetylation ,Protein Tyrosine Phosphatase, Non-Receptor Type 11 ,Computational biology ,Biology ,Article ,03 medical and health sciences ,lipidome ,0302 clinical medicine ,Metabolomics ,proteogenomic ,Humans ,Phosphorylation ,EP300 ,proteomic ,Proteogenomics ,acetylome ,single nuclei RNA-seq ,Brain Neoplasms ,Phospholipase C gamma ,glioblastoma ,Computational Biology ,Lipidome ,030104 developmental biology ,Histone ,Oncology ,Acetylation ,030220 oncology & carcinogenesis ,Mutation ,biology.protein ,metabolome ,signaling - Abstract
Glioblastoma (GBM) is the most aggressive nervous system cancer. Understanding its molecular pathogenesis is crucial to improving diagnosis and treatment. Integrated analysis of genomic, proteomic, post-translational modification and metabolomic data on 99 treatment-naive GBMs provides insights to GBM biology. We identify key phosphorylation events (e.g., phosphorylated PTPN11 and PLCG1) as potential switches mediating oncogenic pathway activation, as well as potential targets for EGFR-, TP53-, and RB1-altered tumors. Immune subtypes with distinct immune cell types are discovered using bulk omics methodologies, validated by snRNA-seq, and correlated with specific expression and histone acetylation patterns. Histone H2B acetylation in classical-like and immune-low GBM is driven largely by BRDs, CREBBP, and EP300. Integrated metabolomic and proteomic data identify specific lipid distributions across subtypes and distinct global metabolic changes in IDH-mutated tumors. This work highlights biological relationships that could contribute to stratification of GBM patients for more effective treatment. Wang et al. perform integrated proteogenomic analysis of adult glioblastoma (GBM), including metabolomics, lipidomics, and single nuclei RNA-Seq, revealing insights into the immune landscape of GBM, cell-specific nature of EMT signatures, histone acetylation in classical GBM, and the existence of signaling hubs which could provide therapeutic vulnerabilities.
- Published
- 2021
16. Hybridization of antisense oligonucleotides with the 3'part of tRNA(Phe).
- Author
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Petyuk VA, Zenkova MA, Giege R, and Vlassov VV
- Subjects
- Base Sequence, Electrophoresis, Polyacrylamide Gel, Molecular Sequence Data, Nucleic Acid Conformation, Oligodeoxyribonucleotides genetics, RNA, Fungal genetics, Ribonuclease H metabolism, Nucleic Acid Hybridization genetics, Oligonucleotides, Antisense genetics, RNA, Transfer, Phe genetics
- Abstract
The interaction of antisense oligodeoxyribonucleotides with yeast tRNA(Phe) was investigated. 14-15-mers complementary to the 3'-terminal sequence including the ACCA end bind to the tRNA under physiological conditions. At low oligonucleotide concentrations the binding occurs at the unique complementary site. At higher oligonucleotide concentrations, the second oligonucleotide molecule binds to the complex due to non-perfect duplex formation in the T-loop stabilized by stacking between the two bound oligonucleotides. In these complexes the acceptor stem is open and the 5'-terminal sequence of the tRNA is accessible for binding of a complementary oligonucleotide. The results prove that the efficient binding of oligonucleotides to the 3'-terminal sequence of the tRNA occurs through initial binding to the single-stranded sequence ACCA followed by invasion in the acceptor stem and strand displacement.
- Published
- 1999
- Full Text
- View/download PDF
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