scholarly article | Q13442814 |
P819 | ADS bibcode | 2015NatCo...6.8861B |
P356 | DOI | 10.1038/NCOMMS9861 |
P932 | PMC publication ID | 4660218 |
P698 | PubMed publication ID | 26572969 |
P5875 | ResearchGate publication ID | 284165742 |
P50 | author | Robert B. Best | Q41049035 |
Andrea Soranno | Q42316865 | ||
Benjamin Schuler | Q42316868 | ||
P2093 | author name string | Alessandro Borgia | |
Jane Clarke | |||
Daniel Nettels | |||
Madeleine B Borgia | |||
Bengt Wunderlich | |||
Katherine R Kemplen | |||
Sarah Shammas | |||
P2860 | cites work | Protein folding funnels: a kinetic approach to the sequence-structure relationship | Q24563939 |
Antibody domain exchange is an immunological solution to carbohydrate cluster recognition | Q27641517 | ||
Different 3D domain-swapped oligomeric cyanovirin-N structures suggest trapped folding intermediates | Q27677513 | ||
Intermolecular domain swapping induces intein-mediated protein alternative splicing | Q27685412 | ||
Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity | Q27733375 | ||
GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation | Q27860944 | ||
Protein misfolding, functional amyloid, and human disease | Q28131732 | ||
Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering | Q28203415 | ||
The immunoglobulin fold. Structural classification, sequence patterns and common core | Q28239187 | ||
Domain-swapped dimer of Pseudomonas aeruginosa cytochrome c551: structural insights into domain swapping of cytochrome c family proteins | Q30373495 | ||
A kinetic study of domain swapping of Protein L | Q87021524 | ||
A microfluidic mixing system for single-molecule measurements | Q45135920 | ||
A native to amyloidogenic transition regulated by a backbone trigger | Q46954596 | ||
Comparison of the transition states for folding of two Ig-like proteins from different superfamilies. | Q51600841 | ||
Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. | Q52856652 | ||
Engineered assembly of intertwined oligomers of an immunoglobulin chain. | Q53938638 | ||
The Immunoglobulin Fold | Q55932791 | ||
THE weighted histogram analysis method for free-energy calculations on biomolecules. I. The method | Q56157177 | ||
Topological Determinants of Protein Domain Swapping | Q57829304 | ||
Hidden complexity in the mechanical properties of titin | Q59061835 | ||
Reverse engineering of the giant muscle protein titin | Q59085863 | ||
Folding studies of immunoglobulin-like β-sandwich proteins suggest that they share a common folding pathway | Q60162505 | ||
Understanding Thermodynamic Competitivity between Biopolymer Folding and Misfolding under Large-Scale Intermolecular Interactions | Q62366791 | ||
Protein interactions with urea and guanidinium chloride. A calorimetric study | Q67493188 | ||
The evolving role of 3D domain swapping in proteins | Q80421566 | ||
Three-dimensional domain swapping in the protein structure space | Q30414200 | ||
Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy | Q30478703 | ||
Insight into the structure of amyloid fibrils from the analysis of globular proteins | Q33266804 | ||
Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state | Q33948562 | ||
Macromolecular crowding: an important but neglected aspect of the intracellular environment | Q34141548 | ||
Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy | Q34154877 | ||
A mechanistic model for amorphous protein aggregation of immunoglobulin-like domains. | Q34334001 | ||
Structural, evolutionary, and assembly principles of protein oligomerization | Q34344086 | ||
The amyloid state and its association with protein misfolding diseases. | Q34421102 | ||
The importance of sequence diversity in the aggregation and evolution of proteins | Q34474861 | ||
Frustration in biomolecules | Q34635987 | ||
Experimental evidence for the role of domain swapping in the evolution of the histone fold | Q35170812 | ||
Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins | Q35177787 | ||
The family feud: do proteins with similar structures fold via the same pathway? | Q36046430 | ||
Frustration in the energy landscapes of multidomain protein misfolding | Q36582991 | ||
Protein acrobatics in pairs--dimerization via domain swapping | Q37177524 | ||
Free energy landscapes for initiation and branching of protein aggregation | Q37409306 | ||
Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins | Q37469603 | ||
Domain swapping is a consequence of minimal frustration | Q37535259 | ||
Implications of 3D domain swapping for protein folding, misfolding and function. | Q38040726 | ||
Systemic amyloidoses | Q38085664 | ||
Immunoglobulin light chain amyloidosis | Q38172295 | ||
The origins of asymmetry in the folding transition states of protein L and protein G. | Q38270380 | ||
From molecule to molecule and cell to cell: prion-like mechanisms in amyotrophic lateral sclerosis. | Q38363338 | ||
Domain swapping and amyloid fibril conformation. | Q42241154 | ||
Interactions crucial for three-dimensional domain swapping in the HP-RNase variant PM8. | Q42811142 | ||
Plasticity within the obligatory folding nucleus of an immunoglobulin-like domain | Q43110554 | ||
Titin; a multidomain protein that behaves as the sum of its parts | Q43866956 | ||
Microfluidic mixer designed for performing single-molecule kinetics with confocal detection on timescales from milliseconds to minutes | Q44589111 | ||
Protein oligomerization through domain swapping: role of inter-molecular interactions and protein concentration | Q44966308 | ||
P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
P6216 | copyright status | copyrighted | Q50423863 |
P407 | language of work or name | English | Q1860 |
P921 | main subject | protein folding | Q847556 |
P304 | page(s) | 8861 | |
P577 | publication date | 2015-11-17 | |
P1433 | published in | Nature Communications | Q573880 |
P1476 | title | Transient misfolding dominates multidomain protein folding | |
P478 | volume | 6 |
Q91602637 | 3D printed selectable dilution mixer pumps |
Q42576606 | A Simple Model of Protein Domain Swapping in Crowded Cellular Environments |
Q50989054 | A critical comparison of coarse-grained structure-based approaches and atomic models of protein folding. |
Q38852916 | A glass menagerie of low complexity sequences. |
Q51127983 | Amorphous protein aggregation monitored using fluorescence self-quenching. |
Q39601498 | An Internal Disulfide Locks a Misfolded Aggregation-prone Intermediate in Cataract-linked Mutants of Human γD-Crystallin |
Q39242034 | Cooperativity and modularity in protein folding |
Q38702791 | Different amyloid aggregation of smooth muscles titin in vitro. |
Q92565293 | Differential proteostatic regulation of insoluble and abundant proteins |
Q92647552 | Evolutionary drivers of protein shape |
Q58570370 | Folding pathway of an Ig domain is conserved on and off the ribosome |
Q49609043 | Isolation and characterization of a minimal building block of polyubiquitin fibrils. |
Q60922145 | Living in Promiscuity: The Multiple Partners of Alpha-Synuclein at the Synapse in Physiology and Pathology |
Q36599493 | Markov state models of protein misfolding |
Q90316268 | Monitoring Unfolding of Titin I27 Single and Bi Domain with High-Pressure NMR Spectroscopy |
Q41319968 | Onset of disorder and protein aggregation due to oxidation-induced intermolecular disulfide bonds: case study of RRM2 domain from TDP-43. |
Q42105214 | Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation |
Q47591511 | Protein folding transition path times from single molecule FRET. |
Q28817241 | Protein knotting through concatenation significantly reduces folding stability |
Q39809462 | Smooth muscle titin forms in vitro amyloid aggregates. |
Q89356208 | Spontaneous refolding of the large multidomain protein malate synthase G proceeds through misfolding traps |
Q36013275 | Structural Determinants of Misfolding in Multidomain Proteins |
Q58753045 | Systematic mapping of free energy landscapes of a growing filamin domain during biosynthesis |
Q60448555 | TADOSS: computational estimation of tandem domain swap stability |
Q60951140 | The Complex Conformational Dynamics of Neuronal Calcium Sensor-1: A Single Molecule Perspective |
Q51061077 | The folding mechanism and key metastable state identification of the PrP127-147 monomer studied by molecular dynamics simulations and Markov state model analysis. |
Search more.