Year |
Citation |
Score |
2019 |
Hermida D, Mortuza GB, Pedersen AK, Pozdnyakova I, Nguyen TTTN, Maroto M, Williamson M, Ebersole T, Cazzamali G, Rand KD, Olsen JV, Malumbres M, Montoya G. Molecular Basis of the Mechanisms controlling MASTL. Molecular & Cellular Proteomics : McP. PMID 31852836 DOI: 10.1074/Mcp.Ra119.001879 |
0.33 |
|
2019 |
Molina R, Stella S, Feng M, Sofos N, Jauniskis V, Pozdnyakova I, López-Méndez B, She Q, Montoya G. Structure of Csx1-cOA complex reveals the basis of RNA decay in Type III-B CRISPR-Cas. Nature Communications. 10: 4302. PMID 31541109 DOI: 10.1038/S41467-019-12244-Z |
0.326 |
|
2016 |
Vernet E, Popa G, Pozdnyakova I, Rasmussen JE, Grohganz H, Giehm L, Jensen MH, Wang H, Plesner B, Nielsen HM, Jensen KJ, Berthelsen J, Sundström M, van de Weert M. Large-scale Biophysical Evaluation of Protein PEGylation Effects: in vitro Properties of 61 Protein Entities. Molecular Pharmaceutics. PMID 27043713 DOI: 10.1021/Acs.Molpharmaceut.6B00049 |
0.356 |
|
2014 |
Wisniewska M, Happonen L, Kahn F, Varjosalo M, Malmström L, Rosenberger G, Karlsson C, Cazzamali G, Pozdnyakova I, Frick IM, Björck L, Streicher W, Malmström J, Wikström M. Functional and structural properties of a novel protein and virulence factor (Protein sHIP) in Streptococcus pyogenes. The Journal of Biological Chemistry. 289: 18175-88. PMID 24825900 DOI: 10.1074/Jbc.M114.565978 |
0.36 |
|
2010 |
Pozdnyakova I, Wittung-Stafshede P. Non-linear effects of macromolecular crowding on enzymatic activity of multi-copper oxidase. Biochimica Et Biophysica Acta. 1804: 740-4. PMID 19932772 DOI: 10.1016/J.Bbapap.2009.11.013 |
0.551 |
|
2005 |
Pozdnyakova I, Regan L. New insights into Fragile X syndrome. Relating genotype to phenotype at the molecular level. The Febs Journal. 272: 872-8. PMID 15670167 DOI: 10.1111/J.1742-4658.2004.04527.X |
0.329 |
|
2004 |
Marks J, Pozdnyakova I, Guidry J, Wittung-Stafshede P. Methionine-121 coordination determines metal specificity in unfolded Pseudomonas aeruginosa azurin Journal of Biological Inorganic Chemistry. 9: 281-288. PMID 14758526 DOI: 10.1007/S00775-004-0523-6 |
0.597 |
|
2003 |
Pozdnyakova I, Wittung-Stafshede P. Approaching the speed limit for Greek Key β-barrel formation: Transition-state movement tunes folding rate of zinc-substituted azurin Biochimica Et Biophysica Acta - Proteins and Proteomics. 1651: 1-4. PMID 14499583 DOI: 10.1016/S1570-9639(03)00240-1 |
0.629 |
|
2002 |
Pozdnyakova I, Wittung-Stafshede P. If space is provided, bulky modification on the rim of Azurin's β-barrel results in folded protein Febs Letters. 531: 209-214. PMID 12417314 DOI: 10.1016/S0014-5793(02)03505-6 |
0.584 |
|
2002 |
Pozdnyakova I, Guidry J, Wittung-Stafshede P. Studies of Pseudomonas aeruginosa azurin mutants: Cavities in β-barrel do not affect refolding speed Biophysical Journal. 82: 2645-2651. PMID 11964251 DOI: 10.1016/S0006-3495(02)75606-3 |
0.613 |
|
2001 |
Pozdnyakova I, Wittung-Stafshede P. Copper binding before polypeptide folding speeds up formation of active (holo) Pseudomonas aeruginosa azurin Biochemistry. 40: 13728-13733. PMID 11695922 DOI: 10.1021/Bi011591O |
0.634 |
|
2001 |
Pozdnyakova I, Wittung-Stafshede P. Biological relevance of metal binding before protein folding [19] Journal of the American Chemical Society. 123: 10135-10136. PMID 11592908 DOI: 10.1021/Ja016252X |
0.558 |
|
2001 |
Pozdnyakova I, Guidry J, Wittung-Stafshede P. Copper stabilizes azurin by decreasing the unfolding rate Archives of Biochemistry and Biophysics. 390: 146-148. PMID 11368526 DOI: 10.1006/Abbi.2000.2369 |
0.559 |
|
2001 |
Pozdnyakova I, Guidry J, Wittung-Stafshede P. Probing copper ligands in denatured Pseudomonas aeruginosa azurin: Unfolding His117Gly and His46Gly mutants Journal of Biological Inorganic Chemistry. 6: 182-188. PMID 11293412 DOI: 10.1007/S007750000189 |
0.611 |
|
2000 |
Pozdnyakova I, Guidry J, Wittung-Stafshede P. Copper-triggered β-hairpin formation initiation site for azurin folding? [26] Journal of the American Chemical Society. 122: 6337-6338. DOI: 10.1021/Ja0011010 |
0.569 |
|
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