Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation

Search Page

Filters

My NCBI Filters

Results by year

Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1952 1
1993 1
2001 1
2010 1
2011 1
2016 3
2018 2
2019 4
2024 0

Text availability

Article attribute

Article type

Publication date

Search Results

13 results

Results by year

Filters applied: . Clear all
Your search was processed without automatic term mapping because it retrieved zero results.
Page 1
Near-Infrared Fluorescent Proteins and Their Applications.
Karasev MM, Stepanenko OV, Rumyantsev KA, Turoverov KK, Verkhusha VV. Karasev MM, et al. Biochemistry (Mosc). 2019 Jan;84(Suppl 1):S32-S50. doi: 10.1134/S0006297919140037. Biochemistry (Mosc). 2019. PMID: 31213194 Review.
Charge transfer process determines ultrafast excited state deactivation of thioflavin T in low-viscosity solvents.
Stsiapura VI, Maskevich AA, Tikhomirov SA, Buganov OV. Stsiapura VI, et al. J Phys Chem A. 2010 Aug 19;114(32):8345-50. doi: 10.1021/jp105186z. J Phys Chem A. 2010. PMID: 20666477
.; Maskevich, A. A.; Kuzmitsky, V. A.; Uversky, V. N.; Kuznetsova, I. M.; Turoverov, K. K. J. Phys. Chem. B 2008, 112, 15893-15902)....
.; Maskevich, A. A.; Kuzmitsky, V. A.; Uversky, V. N.; Kuznetsova, I. M.; Turoverov, K. K. J. Phys. Chem. B 2008, 112, …
The actin/actin interactions involving the N-terminus of the DNase-I-binding loop are crucial for stabilization of the actin filament.
Khaitlina SY, Moraczewska J, Strzelecka-Gołaszewska H. Khaitlina SY, et al. Eur J Biochem. 1993 Dec 15;218(3):911-20. doi: 10.1111/j.1432-1033.1993.tb18447.x. Eur J Biochem. 1993. PMID: 8281943 Free article.
., Collins, J. H., Kuznetsova, I.M., Pershina, V.P., Synakevich, I.G., Turoverov, K.K. & Usmanova, A.M. (1991) FEBS Lett. 279, 49-51]. The resulting C-terminal and N-terminal fragments remained associated to one another in the presence of either Ca2+ or M …
., Collins, J. H., Kuznetsova, I.M., Pershina, V.P., Synakevich, I.G., Turoverov, K.K. & Usmanova, A.M. (1991) FEBS …
The unfolding of iRFP713 in a crowded milieu.
Stepanenko OV, Stepanenko OV, Kuznetsova IM, Turoverov KK. Stepanenko OV, et al. PeerJ. 2019 Apr 8;7:e6707. doi: 10.7717/peerj.6707. eCollection 2019. PeerJ. 2019. PMID: 30993043 Free PMC article.
Two Novel Amyloid Proteins, RopA and RopB, from the Root Nodule Bacterium Rhizobium leguminosarum.
Kosolapova AO, Belousov MV, Sulatskaya AI, Belousova ME, Sulatsky MI, Antonets KS, Volkov KV, Lykholay AN, Shtark OY, Vasileva EN, Zhukov VA, Ivanova AN, Zykin PA, Kuznetsova IM, Turoverov KK, Tikhonovich IA, Nizhnikov AA. Kosolapova AO, et al. Biomolecules. 2019 Nov 4;9(11):694. doi: 10.3390/biom9110694. Biomolecules. 2019. PMID: 31690032 Free PMC article.
Folding of poly-amino acids and intrinsically disordered proteins in overcrowded milieu induced by pH change.
Fonin AV, Stepanenko OV, Sitdikova AK, Antifeeva IA, Kostyleva EI, Polyanichko AM, Karasev MM, Silonov SA, Povarova OI, Kuznetsova IM, Uversky VN, Turoverov KК. Fonin AV, et al. Int J Biol Macromol. 2019 Mar 15;125:244-255. doi: 10.1016/j.ijbiomac.2018.12.038. Epub 2018 Dec 5. Int J Biol Macromol. 2019. PMID: 30529354
pH-induced structural changes of the synthetic homopolypeptides poly-E, poly-K, poly-R, and intrinsically disordered proteins (IDPs) prothymosin alpha (ProTalpha) and linker histone H1, in concentrated PEG solutions simulating macromolecular crowding conditions within the …
pH-induced structural changes of the synthetic homopolypeptides poly-E, poly-K, poly-R, and intrinsically disordered proteins (IDPs) …
Interaction of thioflavin T with amyloid fibrils: stoichiometry and affinity of dye binding, absorption spectra of bound dye.
Sulatskaya AI, Kuznetsova IM, Turoverov KK. Sulatskaya AI, et al. J Phys Chem B. 2011 Oct 6;115(39):11519-24. doi: 10.1021/jp207118x. Epub 2011 Sep 14. J Phys Chem B. 2011. PMID: 21863870
These binding modes have significantly different binding constants (K(b1) = 7.5 10(6) M(-1), K(b2) = 5.6 10(4) M(-1)) and a different number of dye binding sites on the amyloid fibrils per protein molecule (n(1) = 0.11, n(2) = 0.24). ...
These binding modes have significantly different binding constants (K(b1) = 7.5 10(6) M(-1), K(b2) = 5.6 10(4) M(-1)) and a di …
13 results