Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Lubica, Urbanikova"'
Autor:
Lubica Urbanikova, Satoshi Imura, John Landua, J. Martin Scholtz, Bret A. Shirley, C. Nick Pace, D Schell, Saul R. Trevino, Gerald R. Grimsley, Hailong Fu, Jozef Sevcik, Richard L. Thurlkill, Eric J. Hebert, Kazufumi Takano, Ketan S. Gajiwala, Jeffery K. Myers, Katrina Lee Fryar
Publikováno v:
Protein Science. 23:652-661
Our goal was to gain a better understanding of the contribution of the burial of polar groups and their hydrogen bonds to the conformational stability of proteins. We measured the change in stability, Δ(ΔG), for a series of hydrogen bonding mutants
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f1256f62f93690feba03e44988085071
https://doi.org/10.1002/pro.2449
https://doi.org/10.1002/pro.2449
Autor:
C Nick, Pace, Hailong, Fu, Katrina, Lee Fryar, John, Landua, Saul R, Trevino, David, Schell, Richard L, Thurlkill, Satoshi, Imura, J Martin, Scholtz, Ketan, Gajiwala, Jozef, Sevcik, Lubica, Urbanikova, Jeffery K, Myers, Kazufumi, Takano, Eric J, Hebert, Bret A, Shirley, Gerald R, Grimsley
Publikováno v:
Protein science : a publication of the Protein Society. 23(5)
Our goal was to gain a better understanding of the contribution of the burial of polar groups and their hydrogen bonds to the conformational stability of proteins. We measured the change in stability, Δ(ΔG), for a series of hydrogen bonding mutants
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::16a89efc90238769aa0f3ab3cabf1b84
https://pubmed.ncbi.nlm.nih.gov/24591301
https://pubmed.ncbi.nlm.nih.gov/24591301
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 58:1368-1370
Plectin is an abundantly expressed cytoskeletal crosslinking protein of enormous size (>500 kDa) and multiple functions. It represents one of the many members of a large family of actin-binding proteins. The actin-binding domain of mouse plectin was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38add43a4a252e0a2440c86fe5063288
https://doi.org/10.1107/s0907444902010120
https://doi.org/10.1107/s0907444902010120
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 57:737-739
RNase Sa3 produced by Streptomyces aureofaciens strain CCM 3239 belongs to the T1 family of microbial ribonucleases. It is closely related both to RNase Sa, studied in detail earlier, and to RNase Sa2 produced by the same microorganism. The most impo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::292108c5b2d74398457c98a38400ae46
https://doi.org/10.1107/s0907444901003456
https://doi.org/10.1107/s0907444901003456
Autor:
Natalia Csokova, Lubica Urbanikova, Rostislav Skrabana, Michal Novak, Jozef Sevcik, Alexander Popov, Branislav Kovacech
Publikováno v:
Protein and peptide letters 13, 944 (2006). doi:10.2174/092986606778256180
Monoclonal antibody (mAb) MN423 recognizes Alzheimer's disease specific conformation of tau protein assembled into paired helical filaments (PHF). Since the three-dimensional structure of PHF is currently unavailable, the structure of MN423 binding s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bd17f9367f66b890d42f3fee281f4f2
https://pubmed.ncbi.nlm.nih.gov/17100650
https://pubmed.ncbi.nlm.nih.gov/17100650
Autor:
Gregory D. Reinhart, Mauricio Lasagna, J. Martin Scholtz, Lubica Urbanikova, Jozef Sevcik, Roy W. Alston, C. Nick Pace
Publikováno v:
Biophysical journal. 87(6)
Ribonuclease Sa (RNase Sa) contains no tryptophan (Trp) residues. We have added single Trp residues to RNase Sa at sites where Trp is found in four other microbial ribonucleases, yielding the following variants of RNase Sa: Y52W, Y55W, T76W, and Y81W
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::747c81923f3f84313e0dfbb8107adce0
https://pubmed.ncbi.nlm.nih.gov/15377518
https://pubmed.ncbi.nlm.nih.gov/15377518
Publikováno v:
The Journal of biological chemistry. 277(49)
Ribonuclease (RNase) Sa3 is secreted by the Gram-positive bacterium Streptomyces aureofaciens. The enzyme catalyzes the cleavage of RNA on the 3' side of guanosine residues. Here, x-ray diffraction analysis was used to determine the three-dimensional
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac059d1f4e2fd83c9ef94ca90a6a8ddf
https://pubmed.ncbi.nlm.nih.gov/12228255
https://pubmed.ncbi.nlm.nih.gov/12228255
Autor:
Lubica Urbanikova, Pace Cn, J Bechert, E J Hebert, Jozef Sevcik, J M Scholtz, Kevin L. Shaw, G Horn
Publikováno v:
Journal of molecular biology. 312(2)
The aim of this study was to gain a better understanding of the contribution of hydrogen bonds by tyrosine -OH groups to protein stability. The amino acid sequences of RNases Sa and Sa3 are 69 % identical and each contains eight Tyr residues with sev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e91f2a3def2f20d7cdbe3a01bdcd689
https://pubmed.ncbi.nlm.nih.gov/11554795
https://pubmed.ncbi.nlm.nih.gov/11554795
Publikováno v:
Biochemistry. 37(46)
The contribution of hydrogen bonding by peptide groups to the conformational stability of globular proteins was studied. One of the conserved residues in the microbial ribonuclease (RNase) family is an asparagine at position 39 in RNase Sa, 44 in RNa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1ed191fe38809e02921a467513739a7
https://pubmed.ncbi.nlm.nih.gov/9819211
https://pubmed.ncbi.nlm.nih.gov/9819211
Autor:
Lubica Urbanikova, Jozef Sevcik
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 54(Pt 3)
RNase Sa, an extracellular ribonuclease produced by Streptomyces aureofaciens, is inhibited by barstar, the natural protein inhibitor of barnase, the ribonuclease of Bacillus amyloliquefaciens. The complex of RNase Sa with wild-type barstar was cryst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0684644d8bb9945c4dcfd966d983d16
https://pubmed.ncbi.nlm.nih.gov/9761909
https://pubmed.ncbi.nlm.nih.gov/9761909