Zobrazeno 1 - 10
of 22
pro vyhledávání: '"V N, Uversky"'
Publikováno v:
International review of cell and molecular biology. 329
Misfolding and aggregation of proteins and peptides play an important role in a number of diseases as well as in many physiological processes. Many of the proteins that misfold and aggregate in vivo are intrinsically disordered. Protein aggregation i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::586b0f665f9a4bb57ba9ffbbcfa08e0c
https://pubmed.ncbi.nlm.nih.gov/28109327
https://pubmed.ncbi.nlm.nih.gov/28109327
Publikováno v:
Biofizika. 61(2)
Osmolytes are molecules with the function among others to align hydrostatic pressure between intracellular and extracellular spaces. Accumulation of osmolytes occurs in the cell in response to stress caused by pressure change, change in temperature,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::41cb6fd1ac5ab9ea8b8f5213bdb1c5c3
https://pubmed.ncbi.nlm.nih.gov/27192822
https://pubmed.ncbi.nlm.nih.gov/27192822
Autor:
N. V. Murzina, N. Yu. Protasova, A. G. Murzin, O. I. Gryaznova, M. L. Kireeva, V. N. Uversky, A. T. Gudkov
Publikováno v:
"Protein Engineering, Design and Selection". 7:1373-1377
Three circularly permuted variants of Escherichia coli dihydrofolate reductase genes were constructed. Linkers coding tri- and pentapeptides were used to connect the natural 5'- and 3'-terminal ends. Only one variant of circularly permuted protein wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ebb1888782bef235bb1f13e728a8362
https://doi.org/10.1093/protein/7.11.1373
https://doi.org/10.1093/protein/7.11.1373
Publikováno v:
Current Alzheimer research. 6(3)
To better model the characteristics of crowded intracellular environments, we examined the effect of several factors known to induce partial folding and accelerated fibrillation of alpha-synuclein in dilute solutions, on the fibrillation of this prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::92e8a271f0d3b254687458223a5fa803
https://pubmed.ncbi.nlm.nih.gov/19519306
https://pubmed.ncbi.nlm.nih.gov/19519306
Publikováno v:
ACS Symposium Series ISBN: 9780841239593
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::db91dba769534a470f40649fe6204baf
https://doi.org/10.1021/bk-2006-0935.ch001
https://doi.org/10.1021/bk-2006-0935.ch001
Publikováno v:
ACS Symposium Series ISBN: 9780841239593
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ddc01dd8fa4c5936b3997a3b40ce434d
https://doi.org/10.1021/bk-2006-0935.ch004
https://doi.org/10.1021/bk-2006-0935.ch004
Publikováno v:
Chembiochem : a European journal of chemical biology. 2(11)
GdmCl-, urea-, and pH-induced unfolding pathways of bovine carbonic anhydrase II have been analyzed by using changes induced by different denaturing agents in intensity, anisotropy, life time, and parameter A value of intrinsic fluorescence as well a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2beaa62563e1ec8d754c159ea96cfc1f
https://pubmed.ncbi.nlm.nih.gov/11948867
https://pubmed.ncbi.nlm.nih.gov/11948867
Publikováno v:
The Journal of biological chemistry. 276(47)
Parkinson's disease involves the aggregation of alpha-synuclein to form fibrils, which are the major constituent of intracellular protein inclusions (Lewy bodies and Lewy neurites) in dopaminergic neurons of the substantia nigra. Occupational exposur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::58853fd581893798594c5f0d1b56ff41
https://pubmed.ncbi.nlm.nih.gov/11553618
https://pubmed.ncbi.nlm.nih.gov/11553618
Publikováno v:
Proteins. 41(3)
"Natively unfolded" proteins occupy a unique niche within the protein kingdom in that they lack ordered structure under conditions of neutral pH in vitro. Analysis of amino acid sequences, based on the normalized net charge and mean hydrophobicity, h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e59d28898265fbc84171a7e66845e19c
https://pubmed.ncbi.nlm.nih.gov/11025552
https://pubmed.ncbi.nlm.nih.gov/11025552
Publikováno v:
The Journal of biological chemistry. 275(46)
Time-resolved fluorescence experiments were carried out on a variety of apomyoglobins with one or two tryptophan (Trp) residues located at invariant positions 7 and 14 in the primary sequence. In all cases, the Trp fluorescence kinetics were resolved
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7857ee6a6eeae89678ebab7c2b37e24b
https://pubmed.ncbi.nlm.nih.gov/10948189
https://pubmed.ncbi.nlm.nih.gov/10948189