يعرض 1 - 20 نتائج من 115 نتيجة بحث عن '"O. V. Kovaleva"', وقت الاستعلام: 0.82s تنقيح النتائج
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    المؤلفون: O. V. Kovaleva, L. A. Lityaeva

    المصدر: Детские инфекции (Москва), Vol 20, Iss 2, Pp 44-48 (2021)

    وصف الملف: electronic resource

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    المؤلفون: L. A. Lityaevа, O. V. Kovaleva

    المصدر: Детские инфекции (Москва), Vol 18, Iss 3, Pp 37-41 (2019)

    مصطلحات موضوعية: herpes viruses, newborns, intestinal microbiota, Pediatrics, RJ1-570

    وصف الملف: electronic resource

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    المصدر: Surgery and Oncology; Том 14, № 4 (2024); 86-92 ; Хирургия и онкология; Том 14, № 4 (2024); 86-92 ; 2949-5857

    وصف الملف: application/pdf

    Relation: https://www.onco-surgery.info/jour/article/view/759/487; Sung H., Ferlay J., Siegel R.L. et al. Global cancer statistics 2020: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA Cancer J Clin 2021;71(3):209–49. DOI:10.3322/caac.21660; Заридзе Д.Г., Каприн А.Д., Стилиди И.С. Динамика заболеваемости и смертности от злокачественных новообразований в России. Вопросы онкологии 2018;64(5):578–90.; Герштейн Е.С., Огнерубов Н.А., Чанг В.Л. и др. Растворимые формы PD-1 и PD-L1 в плазме крови больных раком желудка и их связь с клиническими и морфологическими характеристиками заболевания. Клиническая лабораторная диагностика 2020;65(6):347–52. DOI: http://dx.doi.org/10.18821m69-2084-2020-65-6-347-352; Guo Y., Walsh A.M., Canavan M. et al. Immune checkpoint inhibitor PD-1 pathway is down-regulated in synovium at various stages of rheumatoid arthritis disease progression. PLoS ONE 2018;13(2):e0192704. DOI:10.1371/journal.pone.0192704; Theodoraki M.N., Yerneni S.S., Hoffmann T.K. et al. Clinical significance of PD-L1+ exosomes in plasma of head and neck cancer patients. Clin Cancer Res 2018;24(4):896–905. DOI:10.1158/1078-0432.CCR-17-2664; Герштейн Е.С., Уткин Д.О., Горячева И.О. и др. Растворимые формы рецептора контрольной точки иммунитета PD-1 и его лиганда PD-L1 в плазме крови больных новообразованиями яичников. Альманах клинической медицины 2018;46(7):690–8. DOI:10.18786/2072-0505-2018-46-7-690-698; Ковалева О.В., Грачев А.Н., Макарова Э.И. и др. Прогностическая значимость sPD-1/sPD-L1 при раке о почки в зависимости от фенотипа опухолевых и стромальных клеток. Онкоурология 2022;18(2):17–28. DOI:10.17650/1726-9776-2022-18-2-17-28; Guo X., Wang J., Jin J. et al. High serum level of soluble programmed death ligand 1 is associated with a poor prognosis in Hodgkin lymphoma. Transl Oncol 2018;11(3):779–85. DOI:10.1016/j.tranon.2018.03.012; Kim H.J., Park S., Kim K.J., Seong J. Clinical significance of soluble programmed cell death ligand-1 (sPD-L1) in hepatocellular carcinoma patients treated with radiotherapy. Radiother Oncol 2018;129(1):130–5. DOI:10.1016/j.radonc.2017.11.027; Kabir T.F., Chauhan A., Anthony L., Hildebrandt G.C. Immune checkpoint inhibitors in pediatric solid tumors: Status in 2018. Ochsner J 2018;18(4):370–6. DOI:10.31486/toj.18.0055; Shigemori T., Toiyama Y., Okugawa Y. et al. Soluble PD-L1 expression in circulation as a predictive marker for recurrence and prognosis in gastric cancer: direct comparison of the clinical burden between tissue and serum PD-L1 expression. Ann Surg Oncol 2019;26(3):876–83. DOI:10.1245/s10434-018-07112-x; Choi Y.Y., Kim H., Shin S.J. et al. Microsatellite instability and programmed cell death-ligand 1 expression in stage II/III gastric cancer: post hoc analysis of the CLASSIC Randomized Controlled study. Ann Surg 2019;270(2):309–16. DOI:10.1097/SLA.0000000000002803; Niu M., Liu Y., Yi M. et al. Biological characteristics and clinical significance of soluble PD-1/PD-L1 and exosomal PD-L1 in cancer. Front Immunol 2022;13:827921. DOI:10.3389/fimmu.2022.827921; Chmielewska I., Grenda A., Krawczyk P. et al. The influence of plasma sPD-L1 concentration on the effectiveness of immunotherapy in advanced NSCLC patients. Cancer Immunol Immunother 2023;72(12):4169–77. DOI:10.1007/s00262-023-03552-x; Kovaleva O.V., Podlesnaya P.A., Chang V.L. et al. Comprehensive analysis of stromal and serum markers in gastric cancer. Acta Naturae 2022;14(4):75–83. DOI:10.32607/actanaturae.11753.; Shin K., Kim J., Park S.J. et al. Prognostic value of soluble PD-L1 and exosomal PD-L1 in advanced gastric cancer patients receiving systemic chemotherapy. Sci Rep 2023;13:6952. DOI:10.1038/s41598-023-33128-9; Kurosaki T., Chamoto K., Suzuki S. et al. The combination of soluble forms of PD-1 and PD-L1 as a predictive marker of PD-1 blockade in patients with advanced cancers: a multicenter retrospective study. Front Immunol 2023;14:1325462. DOI:10.3389/fimmu.2023.1325462; Kawakami H., Sunakawa Y., Inoue E. et al. Soluble programmed cell death ligand 1 predicts prognosis for gastric cancer patients treated with nivolumab: blood-based biomarker analysis for the DELIVER trial. Eur J Cancer 2023;184:10–20. DOI:10.1016/j.ejca.2023.02.003.

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    المصدر: Cancer Urology; Том 19, № 4 (2023); 24-31 ; Онкоурология; Том 19, № 4 (2023); 24-31 ; 1996-1812 ; 1726-9776

    مصطلحات موضوعية: сыворотка крови, KISS1, blood serum

    وصف الملف: application/pdf

    Relation: https://oncourology.abvpress.ru/oncur/article/view/1724/1492; https://oncourology.abvpress.ru/oncur/article/downloadSuppFile/1724/1408; Kushlinskii N.E., Gershtein E.S., Alferov A.A. et al. Prognostic role of matrix metalloproteinases 2, 7, 8, 9 and their type 1 tissue inhibitor in blood serum of patients with kidney cancer. Bull Exp Biol Med 2020;168(5):673–6. DOI:10.1007/s10517-020-04778-w; Steeg P.S., Ouatas T., Halverson D. et al. Metastasis suppressor genes: basic biology and potential clinical use. Clin Breast Cancer 2003;4(1):51–62. DOI:10.3816/cbc.2003.n.012; Ly T., Harihar S., Welch D.R. KISS1 in metastatic cancer research and treatment: potential and paradoxes. Cancer Metastasis Rev 2020;39(3):739–54. DOI:10.1007/s10555-020-09868-9; Harihar S., Welch D.R. KISS1 metastasis suppressor in tumor dormancy: a potential therapeutic target for metastatic cancers? Cancer Metastasis Rev 2023;42(1):183–96. DOI:10.1007/s10555-023-10090-6; Hu K.L., Chang H.M., Zhao H.C. et al. Potential roles for the kisspeptin/kisspeptin receptor system in implantation and placentation. Hum Reprod Update 2019;25(3):326–43. DOI:10.1093/humupd/dmy046; Wang C.H., Qiao C., Wang R.C., Zhou W.P. KiSS-1-mediated suppression of the invasive ability of human pancreatic carcinoma cells is not dependent on the level of KiSS-1 receptor GPR54. Mol Med Rep 2016;13(1):123–9. DOI:10.3892/mmr.2015.4535; Wang W., Yang Z.L., Liu J.Q. et al. Overexpression of MTA1 and loss of KAI-1 and KiSS-1 expressions are associated with invasion, metastasis, and poor-prognosis of gallbladder adenocarcinoma. Tumori 2014;100(6):667–74. DOI:10.1700/1778.19276; Teng Y., Mei Y., Hawthorn L., Cowell J.K. WASF3 regulates miR-200 inactivation by ZEB1 through suppression of KISS1 leading to increased invasiveness in breast cancer cells. Oncogene 2014;33(2):203–11. DOI:10.1038/onc.2012.565; Zhu N., Zhao M., Song Y. et al. The KiSS-1/GPR54 system: Essential roles in physiological homeostasis and cancer biology. Genes Dis 2022;9(1):28–40. DOI:10.1016/j.gendis.2020.07.008; Ohtaki T., Shintani Y., Honda S. et al. Metastasis suppressor gene KiSS-1 encodes peptide ligand of a G-protein-coupled receptor. Nature 2001;411(6837):613–7. DOI:10.1038/35079135; Kuohung W., Kaiser U.B. GPR54 and KiSS-1: role in the regulation of puberty and reproduction. Rev Endocr Metab Disord 2006;7(4):257–63. DOI:10.1007/s11154-006-9020-2; Francis V.A., Abera A.B., Matjila M. et al. Kisspeptin regulation of genes involved in cell invasion and angiogenesis in first trimester human trophoblast cells. PLoS One 2014;9(6):e99680. DOI:10.1371/journal.pone.0099680; Ciaramella V., Della Corte C.M., Ciardiello F., Morgillo F. Kisspeptin and cancer: molecular interaction, biological functions, and future perspectives. Front Endocrinol (Lausanne) 2018;9:115. DOI:10.3389/fendo.2018.00115; Loosen S.H., Luedde M., Lurje G. et al. Serum levels of kisspeptin are elevated in patients with pancreatic cancer. Dis Markers 2019;2019:5603474. DOI:10.1155/2019/5603474; Canbay E., Ergen A., Bugra D. et al. Kisspeptin-54 levels are increased in patients with colorectal cancer. World J Surg 2012;36(9):2218–24. DOI:10.1007/s00268-012-1636-7; Ergen A., Canbay E., Bugra D. et al. Plasma Kisspeptin-54 levels in gastric cancer patients. Int J Surg 2012;10(9):551–4. DOI:10.1016/j.ijsu.2012.08.014; Gatti L., Rolli L., Corno C. et al. Increased serum levels of KiSS1- derived peptides in non-small cell lung cancer patient liquid biopsies and biological relevance. Transl Lung Cancer Res 2022;11(7):1315–26. DOI:10.21037/tlcr-22-52; Harihar S., Ray S., Narayanan S. et al. Role of the tumor microenvironment in regulating the anti-metastatic effect of KISS1. Clin Exp Metastasis 2020;37(2):209–23. DOI: 0.1007/s10585-020-10030-6; Zheng S., Chang Y., Hodges K.B. et al. Expression of KISS1 and MMP-9 in non-small cell lung cancer and their relations to metastasis and survival. Anticancer Res 2010;30(3):713–8.; https://oncourology.abvpress.ru/oncur/article/view/1724

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    المصدر: Bulletin of Siberian Medicine; Том 22, № 2 (2023); 68-77 ; Бюллетень сибирской медицины; Том 22, № 2 (2023); 68-77 ; 1819-3684 ; 1682-0363 ; 10.20538/1682-0363-2023-22-2

    وصف الملف: application/pdf

    Relation: https://bulletin.ssmu.ru/jour/article/view/5222/3395; https://bulletin.ssmu.ru/jour/article/view/5222/3418; Dumic J., Dabelic S., Flögel M. Galectin-3: an open-ended story. Biochim. Biophys. Acta. 2006;1760(4):616–635. DOI:10.1016/j.bbagen.2005.12.020.; Liu F.T., Hsu D.K. The role of galectin-3 in promotion of the inflammatory response. Drug News Perspect. 2007;20(7):455– 460. DOI:10.1358/dnp.2007.20.7.1149628.; Clementy N., Garcia B., André C., Bisson A., Benhenda N., Pierre B. et al. Galectin-3 level predicts response to ablation and outcomes in patients with persistent atrial fibrillation and systolic heart failure. PLoS One. 2018;13(8):e0201517. DOI:10.1371/journal.pone.0201517.; Asleh R., Enriquez-Sarano M., Jaffe A.S., Manemann S.M., Weston S.A., Jiang R. et al Galectin-3 Levels and Outcomes After Myocardial Infarction: A Population-Based Study. J. Am. Coll. Cardiol. 2019;73(18):2286–2295. DOI:10.1016/j.jacc.2019.02.046.; Chen S.C., Kuo P.L. The role of galectin-3 in the kidneys. Int. J. Mol. Sci. 2016;17(4):565. DOI:10.3390/ijms17040565.; Li Y., Li T., Zhou Z., Xiao Y. Emerging roles of galectin-3 in diabetes and diabetes complications: A snapshot. Rev. Endocr. Metab. Disord. 2022;23(3):569–577. DOI:10.1007/s11154-021-09704-7.; Wang W.H., Lin C.Y., Chang M.R., Urbina A.N., Assavalapsakul W., Thitithanyanont A. et al. The role of galectins in virus infection - A systemic literature review. J. Microbiol. Immunol. Infect. 2020;53(6):925–935. DOI:10.1016/j.jmii.2019. 09.005.; De Oliveira F.L., Gatto M., Bassi N., Luisetto R., Ghirardello A., Punzi L. et al. Galectin-3 in autoimmunity and autoimmune diseases. Exp. Biol. Med. (Maywood). 2015;240(8):1019– 1028. DOI:10.1177/1535370215593826.; Ashraf G.M., Baeesa S.S. Investigation of gal-3 expression pattern in serum and cerebrospinal fluid of patients suffering from neurodegenerative disorders. Front. Neurosci. 2018;12:430. DOI:10.3389/fnins.2018.00430.; Song L., Tang J.W., Owusu L., Sun M.Z., Wu J., Zhang J. Galectin-3 in cancer. Clin. Chim. Acta. 2014;431:185–191. DOI:10.1016/j.cca.2014.01.019.; Xie L., Ni W.K., Chen X.D., Xiao M.B., Chen B.Y., He S. et al. The expressions and clinical significances of tissue and serum galectin-3 in pancreatic carcinoma. J. Cancer Res. Clin. Oncol. 2012;138(6):1035–1043. DOI:10.1007/s00432-012-1178-2.; Matsuda Y., Yamagiwa Y., Fukushima K., Ueno Y., Shimosegawa T. Expression of galectin-3 involved in prognosis of patients with hepatocellular carcinoma. Hepatol. Res. 2008;38(11):1098–1111. DOI:10.1111/j.1872-034X.2008.00387.x.; Kim S.J., Lee S.J., Sung H.J., Choi I.K., Choi C.W., Kim B.S. et al. Increased serum 90K and Galectin-3 expression are associated with advanced stage and a worse prognosis in diffuse large B-cell lymphomas. Acta Haematol. 2008;120(4):211– 216. DOI:10.1159/000193223.; Acikalin M.F., Etiz D., Gurbuz M.K., Ozudogru E., Canaz F., Colak E. Prognostic significance of galectin-3 and cyclin D1 expression in undifferentiated nasopharyngeal carcinoma. Med. Oncol. 2012;29(2):742–749. DOI:10.1007/s12032-011- 9971-3.; Endo K., Kohnoe S., Tsujita E., Watanabe A., Nakashima H., Baba H. et al. Galectin-3 expression is a potent prognostic marker in colorectal cancer. Anticancer Res. 2005;25(4):3117– 3121.; Zhang X.M., Yao G.Y., Zhang B.Y., Wang L.L., Zhao M. [Study on the expression and significance of Galectin-3 and CDC25B mRNA in human gastric carcinoma]. Zhonghua Yi Xue Yi Chuan Xue Za Zhi. 2009;26(3):288–292. (In Chinese). DOI:10.3760/cma.j.issn.1003-9406.2009.03.011.; Yang Z.M., Wu X.T., He T., Da M.X., Luo T., Qian K. [Expression of galectin-3 mRNA in gastric cancer with peritoneal metastasis]. Sichuan Da Xue Xue Bao Yi Xue Ban. 2006;37(1):105–108. (In Chinese).; O’Driscoll L., Linehan R., Liang Y.H., Joyce H., Oglesby I., Clynes M. Galectin-3 expression alters adhesion, motility and invasion in a lung cell line (DLKP), in vitro. Anticancer Res. 2002;22(6A):3117–3125.; Castronovo V., Van Den Brûle F.A., Jackers P., Clausse N., Liu F.T., Gillet C. et al. Decreased expression of galectin-3 is associated with progression of human breast cancer. J. Pathol. 1996;179(1):43–48. DOI:10.1002/(SICI)1096-9896(199605)179:13.0.CO;2-N.; Knapp J.S., Lokeshwar S.D., Vogel U., Hennenlotter J., Schwentner C., Kramer M.W. et al. Galectin-3 expression in prostate cancer and benign prostate tissues: correlation with biochemical recurrence. World J. Urol. 2013;31(2):351–358. DOI:10.1007/s00345-012-0925-y.; Wang Y., Nangia-Makker P., Tait L., Balan V., Hogan V., Pienta K.J. et al. Regulation of prostate cancer progression by galectin-3. Am. J. Pathol. 2009;174(4):1515–1523. DOI:10.2353/ajpath.2009.080816.; Zhou X., Jing J., Peng J., Mao W., Zheng Y., Wang D. et al. Expression and clinical significance of galectin-3 in osteosarcoma. Gene. 2014;546(2):403–407. DOI:10.1016/j.gene.2014.04.066.; Park G.B., Kim D.J., Kim Y.S., Lee H.K., Kim C.W., Hur D.Y. Silencing of galectin-3 represses osteosarcoma cell migration and invasion through inhibition of FAK/Src/Lyn activation and β-catenin expression and increases susceptibility to chemotherapeutic agents. Int. J. Oncol. 2015;46(1):185– 194. DOI:10.3892/ijo.2014.2721.; Dong R., Zhang M., Hu Q., Zheng S., Soh A., Zheng Y. et al. Galectin-3 as a novel biomarker for disease diagnosis and a target for therapy. Int. J. Mol. Med. 2018;41(2):599–614. DOI:10.3892/ijmm.2017.3311.; Crompton B.D., Stewart C., Taylor-Weiner A., Alexe G., Kurek K.C., Calicchio M.L. et al. The genomic landscape of pediatric Ewing sarcoma. Cancer Discov. 2014;4(11):1326– 1341. DOI:10.1158/2159-8290.CD-13-1037.; Huang Z., Ai Z., Li N., Xi H., Gao X., Wang F. et al. Over expression of galectin-3 associates with short-term poor prognosis in stage II colon cancer. Cancer Biomark. 2016;17(4):445– 455. DOI:10.3233/CBM-160661.; Okada K., Shimura T., Suehiro T., Mochiki E., Kuwano H. Reduced galectin-3 expression is an indicator of unfavorable prognosis in gastric cancer. Anticancer Res. 2006;26(2B):1369–1376.; https://bulletin.ssmu.ru/jour/article/view/5222