RAE.RU
Энциклопедия
ИЗВЕСТНЫЕ УЧЕНЫЕ
FAMOUS SCIENTISTS
Биографические данные и фото 17064 выдающихся ученых и специалистов
Логин   Пароль  
Регистрация Забыли пароль?
 

Верхуша Владислав Витальевич

Научная тема: « ФЛУОРЕСЦЕНТНЫЕ МАРКЕРЫ ДЛЯ МОЛЕКУЛЯРНОЙ И КЛЕТОЧНОЙ БИОЛОГИИ: ФЛУОРЕСЦЕНТНЫЕ ТАЙМЕРЫ, ПОСТОЯННО ФЛУОРЕСЦИРУЮЩИЕ И ФОТОАКТИВИРУЕМЫЕ БЕЛКИ »

Научная биография   « Верхуша Владислав Витальевич »

Членство в Российской Академии Естествознания

Специальность: 03.01.03

Год: 2011

Отрасль науки: Биологические науки

Основные научные положения, сформулированные автором на основании проведенных исследований:

  1. Формирование Tyr-содержащих хромофоров красных FP, PAFP и FT происходит через стадию образования синего интермедиата, хромофор которого состоит из имидазольного кольца и N-ацилиминовой группы, не объединенных в систему сопряженных π-связей с фенольным кольцом тирозина 64.
  2. Автокаталитическая трансформация синего интермедиата в красный хромофор может быть замедлена, полностью остановлена или преобразована в фотоиндуцированный процесс методом сайт-направленного мутагенеза. Тем самым был показан путь целенаправленного превращения мономерных FP в PAFP и FT.
  3. Предложен рациональный молекулярный подход, направленный на получение вариантов FP с большим стоксовым сдвигом флуоресценции посредством формирования в них цепей водородных связей для переноса протона в возбуждённом состоянии хромофора.
  4. Созданные в работе FP, PAFP и FT являются оптимизированными маркерами для стандартных методов флуоресцентной микроскопии, микроскопии сверхвысокого разрешения и для флуоресцентной визуализации процессов в тканях животных.
  5. Полученные в работе FP, PAFP и FT с улучшенными спектральными, биохимическими и фотохимическими свойствами позволяют решать ряд новых биологических задач на живых клетках и тканях млекопитающих.

Список опубликованных работ

Обзоры:

1. Петкевич К.Д., Ефременко Е.Н., Верхуша В.В. и Варфоломеев С.Д. Красные флуоресцентные белки и их свойства. Успехи химии 2010, 79: 273-290.

2. Piatkevich K.D. and Verkhusha V.V. Advances in engineering of fluorescent proteins and photoactivatable proteins with red emission. Curr. Opin. Chem. Biol. 2010, 14: 23-29.

3. Stepanenko O.V., Verkhusha V.V., Kuznetsova I.M., Uversky V.N. and Turoverov К.К. Fluorescent proteins as biomarkers and biosensors: throwing color lights on molecular and cellular processes. Curr. Protein Pept. Sci. 2008, 9: 338-369.

4. Степаненко О.В., Верхуша В.В., Кузнецова И.М. и Туроверов К.К. Флуоресцентные белки: физико-химические свойства и использование в клеточной биологии. Цитология 2007, 49: 395-420.

5. Lukyanov K.A., Chudakov D.M., Lukyanov S. and Verkhusha V.V. Photoactivatable fluorescent proteins. Nat. Rev. Mol. Cell Biol. 2005, 6: 885-891.

6. Verkhusha V.V. and Lukyanov K.A. The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins. Nat. Biotechnol. 2004, 22: 289-296.

Главы в книгах:

7. Lyagin I., Gudkov D., Verkhusha V. and Efremenko E. Genetic construct encoding the biosynthesis of N-His6-e-pHluorins-OPH in E.coli cells. In book: Chemical and Biochemical Physics, Kinetics and Thermodynamics: New Perspectives. (Scott P.E., Zaikov G.E., and Kablov V.F., Eds.), 2008, 83-90. Nova Science Publishers, NY, ISBN 1-60456-024-X.

8. Verkhusha V.V., Matz M.V., Sakurai T. and Lukyanov K.A. GFP-like fluorescent proteins and chromoproteins of the class Anthozoa. In book: Protein Structures: Kaleidoscope of Structural Properties and Functions. (Uversky V.N., Ed.). 2003, 405-439. Research Signpost Publishers, ISBN 81-7736-1775.

Статьи:

9. Piatkevich K.D., Malashkevich V.N., Almo S.C. and Verkhusha V.V. Engineering ESPT pathways based on structural analysis of LSSmKate red fluorescent proteins with large Stokes shift. J. Am. Chem. Soc. 2010, 132: 10762-10770.

10. Morozova K.S., Piatkevich K.D., Gould T.G., Zhang J., Bewersdorf J. and Verkhusha V.V. Far-red fluorescent protein excitable with red lasers for flow cytometry and super-resolution STED nanoscopy. Biophys. J. 2010, 99: L13-L15.

11. Subach F.V., Zhang L., Gadella T.W.J., Gurskaya N.G., Lukyanov K.A. and Verkhusha V.V. Red fluorescent protein with reversibly photoswitchable absorbance for photochromic FRET. Chem. Biol. 2010, 17: 745-755.

12. Subach F.M., Patterson G.H., Renz M., Lippincott-Schwartz J. and Verkhusha V.V. Bright monomeric photoactivatable red fluorescent protein for two-color super-resolution sptPALM of live cells. J. Am. Chem. Soc. 2010, 132: 6481-6491.

13. Subach O.M., Malashkevich V.N., Zencheck W.D., Morozova K.S., Piatkevich K.D., Almo S.C. and Verkhusha V.V. Structural characterization of acylimine-containing blue and red chromophores in mTagBFP and TagRFP fluorescent proteins. Chem. Biol. 2010, 17: 333-341.

14. Pletnev S., Subach F.V., Dauter Z., Wlodawer A. and Verkhusha V.V. Understanding blue-to-red conversion in monomeric fluorescent timers and hydrolytic degradation of their chromophores. J. Am. Chem. Soc. 2010, 132: 2243-2253.

15. Piatkevich K.D., Hulit J., Subach O.M., Wu B., Abdulla A., Segall J.E. and Verkhusha V.V. Monomeric red fluorescent proteins with a large Stokes shift. Proc. Natl. Acad. Sci. USA. 2010, 107: 5369-5374.

16. Subach F.V., Malashkevich V.N., Zencheck W.D., Xiao H., Filonov G.S., Almo S.C. and Verkhusha V.V. Photoactivation mechanism of PAmCherry based on crystal structures of the protein in the dark and fluorescent states. Proc. Natl. Acad. Sci. USA. 2009, 106: 21097-21102.

17. Pletnev S., Morozova K.S., Verkhusha V.V. and Dauter Z. Rotational order-disorder structure of fluorescent protein FP480. Acta Crystallogr. D Biol. Crystallogr. 2009, 65: 906-912.

18. He J., Vora M., Haney R.M., Filonov G.S., Musselman C.A., Burd C.G., Kutateladze A.G., Verkhusha V.V., Stahelin R.V. and Kutateladze T.G. Membrane insertion of the FYVE domain is modulated by pH. Proteins 2009, 76: 852-860.

19. Bogdanov A., Mishin A., Yampolsky I., Belousov V., Chudakov D., Subach F., Verkhusha V.V., Lukyanov S. and Lukyanov K.A. Green fluorescent proteins are light-induced electron donors. Nat. Chem. Biol. 2009, 5: 459-461.

20. Shcherbo D., Murphy C.S., Chepurnykh T.V., Shcheglov A.S., Verkhusha V.V., Pletnev V.Z., Hazelwood K.L., Lukyanov S., Davidson M.W. and Chudakov D.M. Far-red fluorescent tags for protein imaging in living tissues. Biochem. J. 2009, 418: 567-574.

21. Telford W.G., Subach F.V. and Verkhusha V.V. Super-continuum white light lasers for flow cytometry. Cytometry 2009, 75A: 450-459.

22. Gould T.J., Verkhusha V.V. and Hess S.T. Imaging biological structures with fluorescence photoactivation localization microscopy. Nat. Protocols 2009, 4: 291-308.

23. Subach F.V., Patterson G.H., Manley S., Gillette J.M., Lippincott-Schwartz J. and Verkhusha V.V. Photoactivatable mCherry for high-resolution two-color fluorescence microscopy. Nat. Methods 2009, 6: 153-159.

24. Subach F.V., Subach O.M., Gundorov I.S., Morozova K.S., Piatkevich K.D., Cuervo A.M. and Verkhusha V.V. Monomeric fluorescent timers that change color from blue to red report on cellular trafficking. Nat. Chem. Biol. 2009, 5: 118-126.

25. Gould T.J., Gunewardene M.S., Gudheti M.V., Verkhusha V.V., Yin S.R., Gosse J.A. and Hess S.T. Nanoscale imaging of molecular positions and anisotropies. Nat. Methods 2008, 5: 1027-1030.

26. Kedrin D., Gligorijevic B., Wyckoff J., Verkhusha V.V., Condeelis J., Segall J.E. and van Rheenen J. Intravital imaging of metastatic behavior through a mammary imaging window. Nat. Methods 2008, 5: 1019-1021.

27. Subach O.M., Gundorov I.S., Yoshimura M., Subach F.V., Zhang J., Grьenwald G., Souslova E.A., Chudakov D.M. and Verkhusha V.V. Conversion of red fluorescent protein into a bright blue probe. Chem. Biol. 2008, 15: 1116-1124.

28. Stepanenko O.V., Verkhusha V.V., Shavlovsky M.M., Kuznetsova I.M., Uversky V.N. and Turoverov K.K. Understanding the role of Arg96 in structure and stability of green fluorescent protein. Proteins 2008, 73: 539-551.

29. Pena P.V., Hom R.A., Hung T., Lin H., Kuo A.J., Wong R.P.C., Subach O.M., Champagne K.S., Zhao R., Verkhusha V.V., Li G., Gozani O. and Kutateladze T.G. Histone H3K4me3 binding is required for the DNA repair and apoptotic activities of ING1 tumor suppressor. J. Mol. Biol. 2008, 380: 303-312.

30. Kapoor V., Karpov V., Linton C., Subach F.V., Verkhusha V.V. and Telford W.G. Solid state yellow and orange lasers for flow cytometry. Cytometry 2008, 73A: 570-577.

31. Mishin A.S., Subach F.V., Yampolsky I.V., King W., Lukyanov K.A. and Verkhusha V.V. The first mutant of the Aequorea victoria green fluorescent protein that forms a red chromophore. Biochemistry 2008; 47: 4666-4673.

32. Hom R.A, Vora M., Regner M., Subach O.M., Cho W., Verkhusha V.V., Stahelin R.V. and Kutateladze T.G. pH-dependent binding of the epsin ENTH domain and the AP180 ANTH domain to PI(4,5)P2-containing bilayers. J. Mol. Biol. 2007, 373: 412-423.

33. Kapoor V., Subach F.V., Kozlov V.G., Grudinin A., Verkhusha V.V. and Telford W.G. New lasers for flow cytometry: filling the gaps. Nat. Methods 2007, 4: 678-679.

34. Невзглядова О.В., Артемов А.В., Зенин В.В., Верхуша В.В., Шавловский М.М., Поварова О.И., Степаненко О.В., Кузнецова И.М. и Туроверов К.К. Экспрессия рекомбинантного актина 5С из дрозофилы в метилотрофных дрожжах Pichia pastoris. Цитология 2007, 49: 300-310.

35. Gurskaya N.G., Verkhusha V.V., Shcheglov A.S., Staroverov D.B., Chepurnykh T.V., Fradkov A.F., Lukyanov S. and Lukyanov K.A. Engineering of a monomeric green-to-red photoactivatable fluorescent protein induced by blue light. Nat. Biotechnol. 2006, 24: 461-465.

36. Lee S.A., Eyeson R., Cheever M.L., Geng J., Verkhusha V.V., Burd C., Overduin M. and Kutateladze T.G. Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch. Proc. Natl. Acad. Sci. USA 2005, 102: 13052-13057.

37. Verkhusha V.V. and Sorkin A. Conversion of the monomeric red fluorescent protein into a photoactivatable probe. Chem. Biol. 2005, 12: 279-285.

38. Stepanenko O.V., Verkhusha V.V., Kazakov V.I., Shavlovsky M.M., Kuznetsova I.M., Uversky V.N. and Turoverov K.K. Comparative studies on the structure and stability of fluorescent proteins EGFP, zFP506, mRFP1, dimer2 and DsRed. Biochemistry 2004, 43: 14913-14923.

39. Galperin E., Verkhusha V.V. and Sorkin A. Three-chromophore FRET microscopy to analyze multiprotein interactions in living cells. Nat. Methods 2004, 1: 209-217.

40. Chudakov D.M., Verkhusha V.V., Staroverov D.B., Lukyanov S. and Lukyanov K.A. Photoswitchable fluorescent label for protein tracking. Nat. Biotechnol. 2004, 22: 1435-1439.

41. Verkhusha V.V., Chudakov D.M., Gurskaya N.G., Lukyanov S. and Lukyanov K.A. Common pathway for the red chromophore formation in the fluorescent proteins and chromoproteins. Chem. Biol. 2004, 11: 845-854.

42. Verkhusha V.V., Pozhitkov A.E., Smirnov S.A., Borst J.W., van Hoek A., Klyachko N.L., Levashov A.V. and Visser A.J. Effect of high pressure and reversed micelles on the fluorescent proteins. Biochim. Biophys. Acta 2003, 1622: 192-195.

43. Verkhusha V.V., Kuznetsova I.M., Stepanenko O.V., Zaraisky A.G., Shavlovsky M.M., Turoverov K.K. and Uversky V.N. High stability of Discosoma DsRed as compared to Aequorea EGFP. Biochemistry 2003, 42: 7879-7884.

44. Bulina M.E., Verkhusha V.V., Staroverov D.B., Chudakov D.M. and Lukyanov K.A. Heterooligomeric tagging diminishes non-specific aggregation of target proteins fused with Anthozoa fluorescent proteins. Biochem. J. 2003, 371: 109-114.

45. Verkhusha V.V., Shavlovsky M.M., Nevzglyadova O.V., Gaivoronsky A.A., Artemov A.V., Stepanenko O.V., Kuznetsova I.M. and Turoverov K.K. Expression of recombinant GFP-actin fusion protein in the methylotrophic yeast Pichia pastoris. FEMS Yeast Res. 2003, 3: 105-111.

46. Fradkov A.F., Verkhusha V.V., Staroverov D.B., Bulina M.E., Yanushevich Y.G., Martynov V.I., Lukyanov S. and Lukyanov K.A. Far-red fluorescent tag for protein labelling. Biochem. J. 2002, 368: 17-21.

47. Верхуша В.В., Аковбян Н.А., Ефременко Е.Н., Варфоломеев С.Д. и Вржещ П.В. Кинетический анализ созревания и денатурации красного флуоресцентного белка DsRed. Биохимия 2001, 66: 1659-1670.

48. Verkhusha V.V., Otsuna H., Awasaki T., Oda H., Tsukita S. and Ito K. An enhanced mutant of red fluorescent protein DsRed for double labeling and developmental timer of neural fiber bundle formation. J. Biol. Chem. 2001, 276: 29621-29624.

49. Vrzheshch P.V., Abovikyan N.A., Varfolomeyev S.D. and Verkhusha V.V. Denaturation and partial renaturation of a tightly tetramerized DsRed protein under mildly acidic conditions. FEBS Letters 2000, 487: 203-208.

50. Варфоломеев С.Д., Ефременко Е.Н., Верхуша В.В. и Вржещ П.В. Синтетические аналоги аминокислот в клетках и белках. Вестн. Моск. Ун-та 2000, 41: 352-354.

51. Verkhusha V.V., Tsukita S. and Oda H. Analysis of cytoskeleton dynamics and cell migration in Drosophila ovaries using GFP-actin and E-cadherin-GFP fusion molecules. Proc. SPIE 1999, 3604: 130-139.

52. Verkhusha V.V., Tsukita S. and Oda H. Actin dynamics in lamellipodia of migrating border cells in the Drosophila ovaries revealed by a GFP-actin fusion protein. FEBS Letters 1999, 445: 395-401.

Комментарии:

RobertAbone
08:37, 1 декабря 2017
Doctor Who is now considered a British Institute and has come a long way since it first aired on November 23rd 1963. The very first show saw the Doctor travel 100,00 years into the past to help some dim cavemen discover light. After 26 seasons and seven Doctors later the series came off our screens in 1989 much to the disappointment of the huge devoted fanbase. In 1996 an attempt was made to revive Doctor Who but it wasnt until June 2005 when it came back with a vengeance with Christopher Eccleston as the ninth Doctor that put the series back on the map as it were. It then went on for 5 years with David Tenant portraying the Doctor until 2010 when Matt Smith took over the role. Today it is still a great family show and has attracted many new fans.
https://www.cialissansordonnancefr24.com/commander-cialis-rapidement/
CaseyBrimb
08:18, 8 октября 2017
Some people, especially those running on busy daily schedules tend to use the pills to help maintain weight since they can not afford to follow all the diet programs. This is not advised. It is recommended that one seek advice from a professional in this field before using the pills. This can save one from many dangers associated with the misuse.

The diet pills should always be taken whole. Some people tend to divide the pills to serve a longer period of time. This is not advised and can lead to ineffectiveness. If it is required that one takes a complete tablet, it means that a certain amount of the ingredients are required to achieve the desired goal. It is also recommended that one does not crush the pill and dissolve it in beverages. Chemicals found in beverages have the potential of neutralizing the desired nutrients in the pill thereby leading to ineffectiveness. The best way to take the tablets is swallowing them whole with a glass of water.

The diet pills speed up the metabolic processes. This is the key factor that leads to the burning of all the fats in the body. This means that one passes out lots of urine, which subsequently leads to dehydration. It is imperative that the user take lots of water round the clock. This will help curb dehydration, which can lead to health problems. In addition to that, water offers the required medium for the function of the nutrients and elimination of the fats.

When buying the review of diet pills, it is imperative that one gets the most recommended dose. People tend to compromise the quality and effectiveness of the tablets due to the variation in cost. The low priced pills depict poor quality, which means their effectiveness is not reliable. Some have also been found to cause health problems. The dose should also be taken as recommended. Over dose will not speed up the process but rather lead to complication. This will increase risk of side effects. If the taking of the pill is forgotten, do not take more to compensate for the lost time.

The diet plan enclosed with the diet pills has also to be followed. According to the requirements, the termination of the diet must be done even with no results. This means your body is irresponsive.
CaseyBrimb
10:31, 2 сентября 2017
Click here>>>

Если вы считаете, что какое-то сообщение нарушает Правила, оскорбляет Вас как личность, несёт заведомо ложную информацию, и должно быть удалено, сообщите нам по адресу sergey@rae.ru

Ваше имя
Текст комментария
Введите число с изображения

Антиспам защита

При добавлении комментария Вы соглашаетесь с пользовательским соглашением