Irina D. Pozdnyakova, Ph.D.
Affiliations: | 2002 | Tulane University, New Orleans, LA, United States |
Area:
BiochemistryGoogle:
"Irina Pozdnyakova"Mean distance: 13271
Parents
Sign in to add mentorPernilla Wittung-Stafshede | grad student | 2002 | Tulane | |
(Folding of azurin: A copper -binding beta-barrel protein.) |
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Publications
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Hermida D, Mortuza GB, Pedersen AK, et al. (2019) Molecular Basis of the Mechanisms controlling MASTL. Molecular & Cellular Proteomics : McP |
Molina R, Stella S, Feng M, et al. (2019) Structure of Csx1-cOA complex reveals the basis of RNA decay in Type III-B CRISPR-Cas. Nature Communications. 10: 4302 |
Vernet E, Popa G, Pozdnyakova I, et al. (2016) Large-scale Biophysical Evaluation of Protein PEGylation Effects: in vitro Properties of 61 Protein Entities. Molecular Pharmaceutics |
Wisniewska M, Happonen L, Kahn F, et al. (2014) Functional and structural properties of a novel protein and virulence factor (Protein sHIP) in Streptococcus pyogenes. The Journal of Biological Chemistry. 289: 18175-88 |
Pozdnyakova I, Wittung-Stafshede P. (2010) Non-linear effects of macromolecular crowding on enzymatic activity of multi-copper oxidase. Biochimica Et Biophysica Acta. 1804: 740-4 |
Pozdnyakova I, Regan L. (2005) New insights into Fragile X syndrome. Relating genotype to phenotype at the molecular level. The Febs Journal. 272: 872-8 |
Marks J, Pozdnyakova I, Guidry J, et al. (2004) Methionine-121 coordination determines metal specificity in unfolded Pseudomonas aeruginosa azurin Journal of Biological Inorganic Chemistry. 9: 281-288 |
Pozdnyakova I, Wittung-Stafshede P. (2003) 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 |
Pozdnyakova I, Wittung-Stafshede P. (2002) If space is provided, bulky modification on the rim of Azurin's β-barrel results in folded protein Febs Letters. 531: 209-214 |
Pozdnyakova I, Guidry J, Wittung-Stafshede P. (2002) Studies of Pseudomonas aeruginosa azurin mutants: Cavities in β-barrel do not affect refolding speed Biophysical Journal. 82: 2645-2651 |