FG nucleoporins feature unique patterns that distinguish them from other IDPs

Free energy calculations shed light on the nuclear pore complex’s selective barrier nature

(2021) Atsushi Matsuda et al.   BIOPHYSICAL JOURNAL

Nucleoporins' exclusive amino acid sequence features regulate their transient interaction with and selectivity of cargo complexes in the nuclear pore

(2021) Mohaddeseh Peyro et al.   MOLECULAR BIOLOGY OF THE CELL

Ion Mobility Mass Spectrometry Uncovers the Impact of the Patterning of Oppositely Charged Residues on the Conformational Distributions of Intrinsically Disordered Proteins

(2019) Rebecca Beveridge et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Structure and Assembly of the Nuclear Pore Complex

(2019) Bernhard Hampoelz et al.   Annual Review of Biophysics

Proteome-wide signatures of function in highly diverged intrinsically disordered regions

(2019) Taraneh Zarin et al.   eLife

Sequence charge decoration dictates coil-globule transition in intrinsically disordered proteins

(2018) Taylor Firman et al.   JOURNAL OF CHEMICAL PHYSICS

Modulating charge patterning and ionic strength as a strategy to induce conformational changes in intrinsically disordered proteins

(2018) Jonathan Huihui et al.   JOURNAL OF CHEMICAL PHYSICS

Selection maintains signaling function of a highly diverged intrinsically disordered region

(2017) Taraneh Zarin et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Single-Molecule FRET Spectroscopy and the Polymer Physics of Unfolded and Intrinsically Disordered Proteins

(2016) Benjamin Schuler et al.   Annual Review of Biophysics

Dancing Protein Clouds: The Strange Biology and Chaotic Physics of Intrinsically Disordered Proteins

(2016) Vladimir N. Uversky   JOURNAL OF BIOLOGICAL CHEMISTRY

Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation

(2016) Erik W. Martin et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

The nuclear pore complex: understanding its function through structural insight

(2016) Martin Beck et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

DisProt 7.0: a major update of the database of disordered proteins

(2016) Damiano Piovesan et al.   NUCLEIC ACIDS RESEARCH

Slide-and-exchange mechanism for rapid and selective transport through the nuclear pore complex

(2016) Barak Raveh et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The selective permeability barrier in the nuclear pore complex

(2016) Christina Li et al.   Nucleus

The selective permeability barrier in the nuclear pore complex

(2016) Christina Li et al.   Nucleus

Rapid Brownian Motion Primes Ultrafast Reconstruction of Intrinsically Disordered Phe-Gly Repeats Inside the Nuclear Pore Complex

(2016) R. Moussavi-Baygi et al.   Scientific Reports

Relating sequence encoded information to form and function of intrinsically disordered proteins

(2015) Rahul K Das et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

A theoretical method to compute sequence dependent configurational properties in charged polymers and proteins

(2015) Lucas Sawle et al.   JOURNAL OF CHEMICAL PHYSICS

Evolutionarily Conserved Sequence Features Regulate the Formation of the FG Network at the Center of the Nuclear Pore Complex

(2015) M. Peyro et al.   Scientific Reports

Nucleoporin's Like Charge Regions Are Major Regulators of FG Coverage and Dynamics Inside the Nuclear Pore Complex

(2015) Mohaddeseh Peyro et al.   PLoS One

Probing the Disordered Domain of the Nuclear Pore Complex through Coarse-Grained Molecular Dynamics Simulations

(2014) Ali Ghavami et al.   BIOPHYSICAL JOURNAL

Nuclear Pore Complex Protein Sequences Determine Overall Copolymer Brush Structure and Function

(2014) David Ando et al.   BIOPHYSICAL JOURNAL

Physical Motif Clustering within Intrinsically Disordered Nucleoporin Sequences Reveals Universal Functional Features

(2013) David Ando et al.   PLoS One

Effect of charge, hydrophobicity, and sequence of nucleoporins on the translocation of model particles through the nuclear pore complex

(2013) Mario Tagliazucchi et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues

(2013) R. K. Das et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

D2P2: database of disordered protein predictions

(2012) Matt E. Oates et al.   NUCLEIC ACIDS RESEARCH

A core subunit of Polycomb repressive complex 1 is broadly conserved in function but not primary sequence

(2012) L. Y. Beh et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy

(2012) H. Hofmann et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

ESpritz: accurate and fast prediction of protein disorder

(2011) Ian Walsh et al.   BIOINFORMATICS

Understanding protein non-folding

(2010) Vladimir N. Uversky et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

A Bimodal Distribution of Two Distinct Categories of Intrinsically Disordered Structures with Separate Functions in FG Nucleoporins

(2010) Justin Yamada et al.   MOLECULAR & CELLULAR PROTEOMICS

Net charge per residue modulates conformational ensembles of intrinsically disordered proteins

(2010) A. H. Mao et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Charge interactions can dominate the dimensions of intrinsically disordered proteins

(2010) S. Muller-Spath et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Charge as a Selection Criterion for Translocation through the Nuclear Pore Complex

(2010) Lucy J. Colwell et al.   PLoS Computational Biology

TOP-IDP-Scale: A New Amino Acid Scale Measuring Propensity for Intrinsic Disorder

(2008) Andrew Campen et al.   PROTEIN AND PEPTIDE LETTERS