Юсифов Талех Насиб оглы

Место рождения

Азербайджан, город Шеки

Дата рождения

27 октября 1956 г.

Образование

Химический факультет, Азербайджанский государственный университет

Ученая степень

Доктор философии по биологии 

Ученое звание

Доцент

Название кандидатской (PhD) диссертации:

-          шифр специальности,

-          наименование специальности

-          название темы

03.00.03 Молекулярная биология, Снижение уровня ограничений, накладываемых плазмидами.

Общее количество опубликованных научных работ:

-          количество научных работ, опубликованных за рубежом:

-          количество статей, опубликованных в журналах, индексируемых и реферируемых в международных базах:

61

59

60

Количество авторских свидетельств и патентов

Подготовка кадров:

-          количество кандидатов наук

1

Основные научные достижения

Проведены важные исследования по изучению структуры и функций белков с использованием методов молекулярной биологии, химии белков, биохимии, кристаллографии, оптических методов и биофизических методов, основанных на исследованиях в растворе. Выполнены исследования биологических сенсоров, взаимодействий белок–лиганд и конформационных изменений белков, индуцированных лигандами, что способствовало пониманию путей передачи (трансдукции) различных сигнальных молекул. Изучены физиологические функции крупных мультибелковых мембран-ассоциированных комплексов и ионных каналов. Последние исследования позволили определить структурные основы механизмов активации ионных каналов и выявить новые биологические функции этих уникальных молекулярных систем.

Названия научных работ

1.  Aliyeva A., Qudretova, F., Aliyeva N., Yusifov, T. (2026) Ion Channels and Regulatory Signals of Heme. European Journal of Biology, Q4. accepted.

2.  Yusifov T., Qudratova F., Aliyeva A. (2025). Cytochrome C-like domain within the human BK channel. International Journal of Molecular Sciences, 26(15), 7053. Q1, Impact Factor: 4.9.

3.  Gudratova F., Aliyeva A., Mahmudova S., Gasimov K., & Yusifov T. (2025). ABTS oxidation reaction as a model of cytochrome c-driven electron transfer. Ukrainian Biochemical Journal, 97(4), 43–51. Q4, Impact Factor: 1.45.

4.  The Potassium Channels are an Important Target in Cancer Therapy.F Gudratova, A Aliyeva, S Mahmudova, K Gasimov, T Yusifov, Nature & Science, International Scientific Journal, 2025 / Volume: 7, Issue: 4 / 82-88

5.  Yusifov T., Qudratova F., Aliyeva A. (2024). Role of bioelectrical signaling networks in tumor growth. American Journal of Biomedical and Life Sciences, 12(5), 83–9

6.    Steccanella F., Savalli N, Yusifov T., Neely A., Olcese R.(2019). How Does the α2δ-1 Subunit Modulate Skeletal CaV1.1 Channels. Biophysical Journal, Vol. 116, p113a

7.   Angelini M., Savalli N., Yusifov T., Olcese R. (2019). Skeletal γ1 Subunit Modulation of Human CaV1. 1 and CaV1. 2 Channels. Biophysical Journal, Vol. 116, p112-113a

8.  3. Yusifov T., Savalli N., Pantazis A., Heinemann S., Hoshi T. Olcese R. (2017).    Carbon Monoxide May Regulate BK slo1 Channel Activity by Partially Disrupting Heme Coordination. Biophysical   Journal, Vol. 112, p112a

9.   Savalli N., Angelini M., Pantazis A., Yusifov T., Neely A., Olcese R. (2016).  Eminence of VSD I in the Voltage-Dependent Inactivation of the Human CaV1.2 Channel. Biophysical Journal Vol.110, p444a

10.  Yusifov T., Savalli N., Heinemann S, Hoshi T., Olcese R. (2015). The Heme Bound Human BK Channel Gating Ring is a CO Sensor, Biophysical Journal, Vol. 108, 122a.

11.  Yusifov T., Savalli N., Park S.,Pantazis A., Olcese  R. (2015). The Role of Met-691 in Heme-Dependent Regulation Supports the Presence of a Cytochrome-C-like Structure in Human BK Channels. Biophysical Journal, Vol.8

12.  Yusifov T., Savalli N., Pantazis, A., Olcese R. (2014) Enzymatic Activity of the Human BK Channel: A   Function Beyond Electrical Signaling, Biophysical Journal, Vol. 106, Issue 2, p535a

13.  Yusifov T., Savalli N., Madhvani R., Gandhi Ch., Olcese R. (2014). The Human Bk Channel Encompasses a Cytochrome C-like Structure Within Its Intracellular Gating Ring Domain.      

14.  Yusifov T., Gandhi Ch., Pantazis, A., Olcese R. (2013). Structural Studies of the Apo and Ca2+-Bound States of the Human BK (SLO1) Channel Gating Ring in Solution. Biophysical       Journal, Vol. 104, Issue 2, p473a

15. Yusifov T ., Gandhi Ch., Pantazis, A., Olcese R.(2013). Structural Studies of the Apo and Ca2+-Bound States of the Human BK (SLO1) Channel Gating Ring in Solution. Biophysical Journal, Vol. 104, Issue 2, p473a

16. Yusifov T., Savalli N., and Olcese, R. (2013). Carbon Monoxide Sensing Properties of the Human BK Channel Gating Ring.

17.  Yusifov T ., Javaherian, AD.,  Heinemann  SH., Hoshi  T., Olcese R.(2012). Evidence for Lipid-Induced Structural Rearrangements in the Human BK (Slo1) Channel Gating Ring. Biophysical Journal, Vol. 102, p688a

18.  Yusifov T., Javaherian, AD. Heinemann, SH., Hoshi, T., Olcese R. (2012). Calcium and Heme Induce Distinct Conformational States of the Human BK (Slo1) Channel Gating Ring. Biophysical Journal, Vol. 102, p687a–

19.   Savalli N., Pantazis A., Yusifov T., Sigg D., and Olcese R. (2012). The contribution of RCK domains to human BK channel allosteric activation.  J Biol. Chem., 287(26):21741-50

20. Yusifov T., Javaherian, AD., Pantazis A., Gandhi Ch. Olcese, R. (2011). Structural & Functional Analysis of the Human BK Channel Gating Ring and its components, RCK1 & RCK2, American Society of Anesthesiologists, Annual Meeting Papers

21. Yusifov T., Javaherian AD, Gandhi Ch. Olcese, R. (2011). On the Properties of the RCK1 Domain of the Human BK (SLO1) Channel.  Biophysical Journal, Vol. 100, Issue 3, p581a

22.  Yusifov T., Javaherian, AD, Pantazis, A., Gandhi Ch., Heinemann, SH.,Hoshi, T., Olcese R. (2011). Heme-Driven Conformational Changes in the Human Slo1 BKCa Channel Gating Ring. Biophysical   Journal, Vol. 98   Issue 3, p126a

23. Javaherian AD., Yusifov T., Pantazis A., Franklin S., Gandhi Ch., Olcese, R. (2011). Metal-driven Operation of the Human Large-conductance Voltage- and Ca2+-dependent     Potassium Channel (BK) Gating Ring Apparatus. J Biol Chem., 286(23): 20701- 19

24. Yusifov T., Javaherian AD., Pantazis A., Gandhi Ch., Olcese R. (2011) The RCK1 domain of the human BKCa channel transduces Ca2+ binding into structural rearrangements.  J Gen. Physiol. 136: 189–202

25.  Javaherian, AD, Yusifov T., Nicole D., Gandhi, Ch., Olcese R. (2010).   The purified BKca Gating Ring binds Ca2+ /Mg 2+, and undergoes a structural change, reflecting the molecular underpinnings of channel   activation. American Society of Anesthesiologists,   Annual Meeting Papers

26. Yusifov T., Javaherian AD., Hou S., Hoshi T., Olcese R. (2010). Heme Induced Structural Rearrangements in the Human BK Channel Intracellular C-Terminus.  American Society of Anesthesiologists, Annual Meeting Papers

27. Yusifov T., Javaherian, AD, Gandhi Ch., Olcese, R. (2009). The Role of Aspartates 362/367 in the Ca 2+ Sensitivity of Human BKCa Channels. American Society of Anesthesiologists, Annual Meeting papers

28. Javaherian, AD., Yusifov T., Nicole D., Gandhi Ch., Olcese, R. (2009). The Intracellular C-Terminus of the Human BKCa Channel Is a Ca 2+ -Binding Tetrameric Domain Structural and Functional Analysis of the Purified Cytosolic C-Terminus of the Human BK Channel. Biophysical Journal, Vol. 96, Issue 3, p481a

29. Javaherian AD., Yusifov T., Nicole D., Gandhi Ch., Olcese, R. (2009). Structural and Functional Analysis of the Purified Cytosolic C- Terminus of the Human BK Channel. Biophysical Journal, Vol. 96,  Issue 3, p481a

30. Javaherian AD., Yusifov T., Nicole D., Gandhi Ch., Olcese, R. (2009). Structural and Functional Analysis of the Purified Cytosolic C-  Terminus of the Human BK Channel. Biophysical Journal, Vol. 96,  Issue 3, p481a

31. Yusifov T., Javaherian AD., Nicole D., Gandhi Ch., Olcese, R. (2009). Calcium Sensing Properties of the RCK1 Domain of the Human BK Channel: Effects of the D362/367A Mutation.  Biophysical   Journal, 

32.  Yusifov T., Abduragimov AR., Gasymov OK., Glasgow BJ. (2008). Tear lipocalin is the major endonuclease in tears. Mol.Vis. 14:180-188.

33. Yusifov T., Savalli N., Ottolia M., and Olcese R. (2008). The RCK2 Domain of the human BKCa channel is calcium sensor. PNAS, 105: 376-381

34. Gasymov OK, Abduragimov AR, Prasher P, Yusifov TN, Glasgow BJ. Tear lipocalin: evidence for a scavenging function to remove lipids from the human corneal surface. Invest Ophthalmol Vis Sci. 2005 Oct;46(10):3589-96. doi: 10.1167/iovs.05-0569. PMID: 16186338; PMCID: PMC1618769.

35.  Gasymov OK., Abduragimov AR., Yusifov T., Glasgow BJ. (2004). Inter-strand   loops CD and EF act as pH-dependent gates to regulate fatty acid ligand binding in tear lipocalin. Biochemistry 43(40): 12894-904.

36.  Glasgow BJ, Gasymov OK, Abduragimov AR, Yusifov TN, Altenbach C, Hubbell WL. Side chain mobility and ligand interactions of the G strand of tear lipocalins by site-directed spin labeling. Biochemistry. 1999 Oct 12;38(41):13707-16. doi: 10.1021/bi9913449. PMID: 10521278.

37.  Gasymov OK., Abduragimov AP., Gasimov EO., Yusifov T., Dooley AK., Glasgow BJ. (2004). Tear lipocalin: potential for selective delivery of rifampin.  Biochim. Biophys. Acta. 1688(2): 102-11.

38. Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Resolving near-ultraviolet circular dichroism spectra of single trp mutants in tear lipocalin. Anal Biochem. 2003 Jul 15;318(2):300-8. doi: 10.1016/s0003-2697(03)00215-x. PMID: 12814635.

39. Gasymov OK., Abduragimov AR., Yusifov T., Glasgow BJ. (2003). Resolving near-ultraviolet circular dichroism spectra of single Trp mutants. Anal Biochem. 318(2): 300-8.

40.  Glasgow BJ, Abduragimov AR, Gasymov OK, Yusifov TN. Tear lipocalin: structure, function and molecular mechanisms of action. Adv Exp Med Biol. 2002;506(Pt A):555-65. doi: 10.1007/978-1-4615-0717-8_78. PMID: 12613960.

41. Glasgow BJ, Abduragimov AR, Gassymov OK, Faull KF, Yusifov TN, Lehrer RI. Characterization of a lipophilin in rabbit tears. Adv Exp Med Biol. 2002;506(Pt A):573-80. doi: 10.1007/978-1-4615-0717-8_80. PMID: 12613962.

42.  Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Relaxation of beta-structure in tear lipocalin and enhancement of retinoid binding. Invest Ophthalmol Vis Sci. 2002 Oct;43(10):3165-73. PMID: 12356820.

43.  Abduragimov AR, Gasymov OK, Yusifov TN, Glasgow BJ. Functional cavity dimensions of tear lipocalin. Curr Eye Res. 2000 Oct;21(4):824-32. doi: 10.1076/ceyr.21.4.824.5551. PMID: 11120574.

44.  Glasgow BJ, Abduragimov AR, Gassymov OK, Yusifov TN, Ruth EC, Faull KF. Vitamin E associated with the lipocalin fraction of human tears. Adv Exp Med Biol. 2002;506(Pt A):567-72. doi: 10.1007/978-1-4615-0717-8_79. PMID: 12613961.

45. Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. RET and anisotropy measurements establish the proximity of the conserved Trp17 to Ile98 and Phe99 of tear lipocalin. Biochemistry. 2002 Jul 16;41(28):8837-48. doi: 10.1021/bi0121003. PMID: 12102626.

46.  Yusifov T., Abduragimov AR., Gasymov OK., Glasgow BJ. (2000). Endonuclease Activity in Lipocalins. Biochem. J. 347(3): 815-819

47.  Abduragimov AR, Gasymov OK, Yusifov TN, Glasgow BJ. Functional cavity dimensions of tear lipocalin. Curr Eye Res. 2000 Oct;21(4):824-32. doi: 10.1076/ceyr.21.4.824.5551. PMID: 11120574.

48.  Glasgow BJ, Marshall G, Gasymov OK, Abduragimov AR, Yusifov TN, Knobler CM. Tear lipocalins: potential lipid scavengers for the corneal surface. Invest Ophthalmol Vis Sci. 1999 Dec;40(13):3100-7. PMID: 10586930.

49.  Zhao C, Nguyen T, Yusifov T, Glasgow BJ, Lehrer RI. Lipophilins: human peptides homologous to rat prostatein. Biochem Biophys Res Commun. 1999 Mar 5;256(1):147-55. doi: 10.1006/bbrc.1999.0274. PMID: 10066439.

50.  Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Interaction of tear lipocalin with lysozyme and lactoferrin. Biochem Biophys Res Commun. 1999 Nov 19;265(2):322-5. doi: 10.1006/bbrc.1999.1668. PMID: 10558865.

51.  Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Binding studies of tear lipocalin: the role of the conserved tryptophan in maintaining structure, stability and ligand affinity. Biochim Biophys Acta. 1999 Aug 17;1433(1-2):307-20. doi: 10.1016/s0167-4838(99)00133-8. PMID: 10515687.

52.  Glasgow BJ, Gasymov OK, Abduragimov AR, Yusifov TN, Altenbach C, Hubbell WL. Side chain mobility and ligand interactions of the G strand of tear lipocalins by site-directed spin labeling. Biochemistry. 1999 Oct 12;38(41):13707-16. doi: 10.1021/bi9913449. PMID: 10521278.

53.  Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Structural changes in human tear lipocalins associated with lipid binding. Biochim Biophys Acta. 1998 Jul 28;1386(1):145-56. doi: 10.1016/s0167-4838(98)00092-2. PMID: 9675263.

54.   Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. (1997). Solution structure by site directed   tryptophan fluorescence in tear lipocalin. Biophys.Res.Commun.,  239; 191          

55.  Yusifov TN, Zavilgelskii GB, Delver EP, Belogurov AA (1987). Alleviation of K-restriction in the   presence of plasmid pKM101 ard+. II. Cloning of the ard gene. Molekulyarnaya   Biologiya, 21: 847-852

56.   Aliyev DA, Muradov AZ, Yusifov TN, Mamedov ACH, Albiov GV. (1986). Studying the   structural organization of chloroplast DNA 1. Obtaining the genomic library of spinach    chloroplast DNA. Izvestiya   Akademii  Nauk Azerbaidzhanskoi SSR Seriya     Biologicheskikh Nauk, 4: 3-7

57.  Belogurov AA, Yusifov TN, Zavilgelskii GB, Kotova VY. (1985). The novel gene(s) Ard of   plasmid pKM101: Alleviation of EcoK-restriction. Molecular General Genetics 198:509-13 

58. Zavilgelskii GB, Mershavka VY, Yusifov TN, Belogurov AA. (1984). Plasmid pKM101 ard+ mediated alleviation of K-restriction of bacteriophage λ; I. General characteristics and localization of the ard gene. Molekulyarnaya Biologiya, 18: 1590-1597.                                                                                           

59.  Braga EA, Yussifov TN, Nosikov V V. Structural organization of rat ribosomal DNAs. Gene. 1982 Dec;20(2):145–56.

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Министерство науки и образования Азербайджанской Республики Институт молекулярной биологии, AZ1073, г. Баку, ул. Иззета Набиева, 11

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