I. Pozdnyakova

发表

Fragile X mental retardation syndrome: structure of the KH1-KH2 domains of fragile X mental retardation protein.

Tommi Kajander, Lynne Regan, L. Regan, 2007, Structure.

Molecular basis of Tousled-Like Kinase 2 activation

J. Olsen, G. Montoya, I. Pozdnyakova, 2018, Nature Communications.

, Streptococcus pyogenes ( Protein sHIP ) in Novel Protein and Virulence Factor Functional and Structural Properties of a Microbiology

Lars Malmström, L. Björck, M. Varjosalo, 2014 .

Molecular Basis of the Mechanisms Controlling MASTL*

M. Malumbres, J. Olsen, G. Montoya, 2019, Molecular & Cellular Proteomics.

Biological relevance of metal binding before protein folding.

I. Pozdnyakova, P. Wittung-Stafshede, 2001, Journal of the American Chemical Society.

Structure of Csx1-cOA4 complex reveals the basis of RNA decay in Type III-B CRISPR-Cas

Mingxia Feng, Rafael Molina, Vykintas Jauniskis, 2019, Nature Communications.

Stability and Folding of Copper-Binding Proteins

I. Pozdnyakova, P. Wittung-Stafshede, 2010 .

Non-linear effects of macromolecular crowding on enzymatic activity of multi-copper oxidase.

I. Pozdnyakova, P. Wittung-Stafshede, 2010, Biochimica et biophysica acta.

Copper stabilizes azurin by decreasing the unfolding rate.

I. Pozdnyakova, P. Wittung-Stafshede, J. Guidry, 2001, Archives of biochemistry and biophysics.

New insights into Fragile X syndrome

L. Regan, I. Pozdnyakova, 2005 .

Identification of differentially expressed proteins in ovarian cancer using high-density protein microarrays

Gil Mor, M. Snyder, M. Hudson, 2007, Proceedings of the National Academy of Sciences.

Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose)

J. Lukas, K. Neelsen, M. Rask, 2015, Nature Communications.

Functional and Structural Properties of a Novel Protein and Virulence Factor (Protein sHIP) in Streptococcus pyogenes *

L. Björck, M. Varjosalo, George A. Rosenberger, 2014, The Journal of Biological Chemistry.

A PTIP–PA1 subcomplex promotes transcription for IgH class switching independently from the associated MLL3/MLL4 methyltransferase complex

Chunaram Choudhary, G. Montoya, A. Nussenzweig, 2016, Genes & development.

A PTIP-PA 1 subcomplex promotes transcription for IgH class switching independently from the associated MLL 3 / MLL 4 methyltransferase complex

Chunaram Choudhary, G. Montoya, A. Nussenzweig, 2016 .

Methionine-121 coordination determines metal specificity in unfolded Pseudomonas aeruginosa azurin

I. Pozdnyakova, P. Wittung-Stafshede, Jessica R. Marks, 2004, JBIC Journal of Biological Inorganic Chemistry.

Approaching the speed limit for Greek Key beta-barrel formation: transition-state movement tunes folding rate of zinc-substituted azurin.

I. Pozdnyakova, P. Wittung-Stafshede, 2003, Biochimica et biophysica acta.

Large-Scale Biophysical Evaluation of Protein PEGylation Effects: In Vitro Properties of 61 Protein Entities.

Knud J Jensen, Holger Grohganz, H. M. Nielsen, 2016, Molecular pharmaceutics.

New insights into Fragile X syndrome. Relating genotype to phenotype at the molecular level.

I. Pozdnyakova, L. Regan, 2005, The FEBS journal.

Copper binding before polypeptide folding speeds up formation of active (holo) Pseudomonas aeruginosa azurin.

I. Pozdnyakova, P. Wittung-Stafshede, 2001, Biochemistry.

Molecular basis of Tousled-Like Kinase 2 activation

J. Olsen, G. Montoya, I. Pozdnyakova, 2018, Nature Communications.

Studies of Pseudomonas aeruginosa azurin mutants: cavities in beta-barrel do not affect refolding speed.

I. Pozdnyakova, P. Wittung-Stafshede, J. Guidry, 2002, Biophysical journal.

Copper-Triggered β-Hairpin Formation: Initiation Site for Azurin Folding?

I. Pozdnyakova, P. Wittung-Stafshede, and Jesse Guidry, 2000 .