scholarly article | Q13442814 |
P356 | DOI | 10.1007/S00018-016-2416-6 |
P8608 | Fatcat ID | release_hqyej2hzyjay3iio277qqxgjli |
P698 | PubMed publication ID | 27838743 |
P50 | author | Vladimir N. Uversky | Q59698496 |
P2093 | author name string | Leonid Breydo | |
Maria Harreguy Alfonso | |||
Marwa Alhothali | |||
Nikolas Santamaria | |||
P2860 | cites work | Prediction of protein binding regions in disordered proteins | Q21145360 |
Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 Concept | Q22061726 | ||
Classification of intrinsically disordered regions and proteins | Q22061736 | ||
Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation | Q24324878 | ||
The Protein Data Bank | Q24515306 | ||
Alternative splicing in concert with protein intrinsic disorder enables increased functional diversity in multicellular organisms | Q24548466 | ||
hTAF(II)68, a novel RNA/ssDNA-binding protein with homology to the pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II | Q24562004 | ||
UniProt: the Universal Protein knowledgebase | Q24598826 | ||
Frequency of the C9orf72 hexanucleotide repeat expansion in patients with amyotrophic lateral sclerosis and frontotemporal dementia: a cross-sectional study | Q24600803 | ||
The STRING database in 2011: functional interaction networks of proteins, globally integrated and scored | Q24607390 | ||
Unconventional translation of C9ORF72 GGGGCC expansion generates insoluble polypeptides specific to c9FTD/ALS | Q24608159 | ||
Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis | Q24619298 | ||
The IntAct molecular interaction database in 2012 | Q24621004 | ||
Protein tandem repeats - the more perfect, the less structured | Q24624818 | ||
Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS | Q24633692 | ||
A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD | Q24634583 | ||
DisProt: the Database of Disordered Proteins | Q24675789 | ||
Alterations in stress granule dynamics driven by TDP-43 and FUS: a link to pathological inclusions in ALS? | Q26777971 | ||
Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis | Q26863439 | ||
Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators | Q27000495 | ||
Solution structure of Apo Cu,Zn superoxide dismutase: role of metal ions in protein folding | Q27641822 | ||
Structures of mouse SOD1 and human/mouse SOD1 chimeras | Q27664114 | ||
Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43 | Q27687574 | ||
The TDP-43 N-terminal domain structure at high resolution | Q27703592 | ||
Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase | Q27729237 | ||
Crystallization and structure determination of bovine profilin at 2.0 A resolution | Q27730841 | ||
The crystal structure of a major allergen from plants | Q27734729 | ||
Functional roles of transiently and intrinsically disordered regions within proteins | Q28085662 | ||
Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis | Q28131672 | ||
Intrinsically disordered protein | Q28191444 | ||
The Database of Interacting Proteins: 2004 update | Q28234998 | ||
The BioGRID interaction database: 2015 update | Q28252221 | ||
Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells | Q28254284 | ||
Comprehensive large-scale assessment of intrinsic protein disorder | Q60787508 | ||
Characterization of renatured profilin purified by urea elution from poly-L-proline agarose columns | Q69425510 | ||
Crystallographic characterization of recombinant human CuZn superoxide dismutase | Q69663958 | ||
Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation | Q70802575 | ||
An essential role for the conserved Glu-133 in the anion interaction with superoxide dismutase | Q72217950 | ||
Predicting Protein Disorder for N-, C-, and Internal Regions | Q73174432 | ||
SnapShot: Cellular bodies | Q79385899 | ||
Role of intrinsic disorder in transient interactions of hub proteins | Q79416219 | ||
Intrinsic disorder in yeast transcriptional regulatory network | Q80353265 | ||
Optimizing long intrinsic disorder predictors with protein evolutionary information | Q81484824 | ||
Familial versus sporadic amyotrophic lateral sclerosis--a false dichotomy? | Q82333999 | ||
Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks | Q82855583 | ||
C9orf72 hexanucleotide repeat expansions as the causative mutation for chromosome 9p21-linked amyotrophic lateral sclerosis and frontotemporal dementia | Q84958100 | ||
Domain architectures and characterization of an RNA-binding protein, TLS | Q28276007 | ||
The RCSB Protein Data Bank: views of structural biology for basic and applied research and education | Q28650443 | ||
Pfam: the protein families database | Q28660698 | ||
A decade and a half of protein intrinsic disorder: biology still waits for physics | Q28681184 | ||
Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis | Q28730723 | ||
The importance of intrinsic disorder for protein phosphorylation | Q28776125 | ||
Human Protein Reference Database--2009 update | Q29547392 | ||
Intrinsically unstructured proteins | Q29614784 | ||
Stress granules: the Tao of RNA triage | Q29615263 | ||
Protein disorder prediction: implications for structural proteomics | Q29615736 | ||
GlobPlot: Exploring protein sequences for globularity and disorder | Q29615737 | ||
Why are "natively unfolded" proteins unstructured under physiologic conditions? | Q29615739 | ||
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm | Q29615865 | ||
IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content | Q29615888 | ||
Intrinsic disorder and protein function | Q29616415 | ||
Natively unfolded proteins: a point where biology waits for physics | Q29616416 | ||
Sequence complexity of disordered protein | Q29616420 | ||
Structural, Functional, and Immunological Characterization of Profilin Panallergens Amb a 8, Art v 4, and Bet v 2. | Q30276728 | ||
Comparing and combining predictors of mostly disordered proteins. | Q30350136 | ||
Exploiting heterogeneous sequence properties improves prediction of protein disorder. | Q30351476 | ||
Flexible nets. The roles of intrinsic disorder in protein interaction networks. | Q30351593 | ||
Length-dependent prediction of protein intrinsic disorder. | Q30353929 | ||
Understanding protein non-folding. | Q30385084 | ||
Intrinsically disordered proteins: a 10-year recap | Q30421421 | ||
Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes | Q33252616 | ||
Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis | Q33649745 | ||
Profilin-1 phosphorylation directs angiocrine expression and glioblastoma progression through HIF-1α accumulation | Q33675114 | ||
PONDR-FIT: a meta-predictor of intrinsically disordered amino acids | Q33902242 | ||
Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases | Q33909288 | ||
A method for simultaneous alignment of multiple protein structures | Q33978603 | ||
FUS-immunoreactive inclusions are a common feature in sporadic and non-SOD1 familial amyotrophic lateral sclerosis | Q34118590 | ||
Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity | Q34141572 | ||
MINT, the molecular interaction database: 2012 update | Q34233947 | ||
Structure and mechanism of copper, zinc superoxide dismutase | Q34255150 | ||
MobiDB: a comprehensive database of intrinsic protein disorder annotations. | Q34278790 | ||
D²P²: database of disordered protein predictions | Q34314929 | ||
The C9orf72 GGGGCC repeat is translated into aggregating dipeptide-repeat proteins in FTLD/ALS. | Q34326849 | ||
Alternative splicing of intrinsically disordered regions and rewiring of protein interactions | Q38109334 | ||
Intrinsically disordered proteins and intrinsically disordered protein regions | Q38194194 | ||
Introducing protein intrinsic disorder | Q38205058 | ||
Subclassifying disordered proteins by the CH-CDF plot method. | Q38499397 | ||
SOD1 in neurotoxicity and its controversial roles in SOD1 mutation-negative ALS. | Q38632098 | ||
Mutant SOD1 mediated pathogenesis of Amyotrophic Lateral Sclerosis | Q38666305 | ||
Dancing Protein Clouds: The Strange Biology and Chaotic Physics of Intrinsically Disordered Proteins | Q38724766 | ||
C9ORF72 Regulates Stress Granule Formation and Its Deficiency Impairs Stress Granule Assembly, Hypersensitizing Cells to Stress | Q38781435 | ||
Insights into the pathogenic mechanisms of Chromosome 9 open reading frame 72 (C9orf72) repeat expansions | Q38789426 | ||
Molecular neuropathology of frontotemporal dementia: insights into disease mechanisms from postmortem studies | Q38866202 | ||
A majority of the cancer/testis antigens are intrinsically disordered proteins | Q39063386 | ||
On the complementarity of the consensus-based disorder prediction. | Q39675172 | ||
Structural diversity and functional implications of the eukaryotic TDP gene family | Q40608660 | ||
Isoform-specific antibodies reveal distinct subcellular localizations of C9orf72 in amyotrophic lateral sclerosis | Q40737530 | ||
Profilin 1 mutants form aggregates that induce accumulation of prion-like TDP-43 | Q41596094 | ||
The phosphatase calcineurin regulates pathological TDP-43 phosphorylation. | Q41628256 | ||
Tissue-specific splicing of disordered segments that embed binding motifs rewires protein interaction networks | Q41884066 | ||
RNA Granules and Diseases: A Case Study of Stress Granules in ALS and FTLD | Q42011097 | ||
C9ORF72 interaction with cofilin modulates actin dynamics in motor neurons | Q42425843 | ||
PrDOS: prediction of disordered protein regions from amino acid sequence | Q42431942 | ||
What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae? | Q42625650 | ||
The structural and functional signatures of proteins that undergo multiple events of post-translational modification | Q42663688 | ||
Characterization of the dipeptide repeat protein in the molecular pathogenesis of c9FTD/ALS. | Q42693496 | ||
Refined solution structure of human profilin I. | Q42844645 | ||
ESpritz: accurate and fast prediction of protein disorder | Q44385437 | ||
Mutation analysis of PFN1 in familial amyotrophic lateral sclerosis patients. | Q45907822 | ||
Faster superoxide dismutase mutants designed by enhancing electrostatic guidance | Q45965859 | ||
The role of arginine 143 in the electrostatics and mechanism of Cu,Zn superoxide dismutase: computational and experimental evaluation by mutational analysis | Q46281486 | ||
Gain-of-function profilin 1 mutations linked to familial amyotrophic lateral sclerosis cause seed-dependent intracellular TDP-43 aggregation | Q46591159 | ||
Evidence of multisystem disorder in whole-brain map of pathological TDP-43 in amyotrophic lateral sclerosis | Q46599359 | ||
Bidirectional transcripts of the expanded C9orf72 hexanucleotide repeat are translated into aggregating dipeptide repeat proteins | Q46797980 | ||
Intrinsic disorder in pathogenic and non-pathogenic microbes: discovering and analyzing the unfoldomes of early-branching eukaryotes | Q47702038 | ||
Coupled folding and binding with alpha-helix-forming molecular recognition elements | Q48122045 | ||
Disorder and sequence repeats in hub proteins and their implications for network evolution. | Q52673882 | ||
The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. | Q52974739 | ||
Phosphorylated TDP-43 becomes resistant to cleavage by calpain: A regulatory role for phosphorylation in TDP-43 pathology of ALS/FTLD. | Q53227139 | ||
Identification of the poly-L-proline-binding site on human profilin. | Q54738745 | ||
A novel phosphorylation site mutation in profilin 1 revealed in a large screen of US, Nordic, and German amyotrophic lateral sclerosis/frontotemporal dementia cohorts. | Q55056826 | ||
Accurate prediction of disorder in protein chains with a comprehensive and empirically designed consensus | Q56992931 | ||
Variable Metallation of Human Superoxide Dismutase: Atomic Resolution Crystal Structures of Cu–Zn, Zn–Zn and As-isolated Wild-type Enzymes | Q57909227 | ||
Analysis of theC9orf72Gene in Patients with Amyotrophic Lateral Sclerosis in Spain and Different Populations Worldwide | Q58006957 | ||
p62 positive, TDP-43 negative, neuronal cytoplasmic and intranuclear inclusions in the cerebellum and hippocampus define the pathology of C9orf72-linked FTLD and MND/ALS | Q58477808 | ||
Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin | Q59080539 | ||
Profilin 1 associates with stress granules and ALS-linked mutations alter stress granule dynamics. | Q34424308 | ||
RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins | Q34425242 | ||
MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins | Q34445775 | ||
The BioPlex Network: A Systematic Exploration of the Human Interactome | Q34485581 | ||
What does it mean to be natively unfolded? | Q34488954 | ||
APID interactomes: providing proteome-based interactomes with controlled quality for multiple species and derived networks. | Q34524369 | ||
Mining alpha-helix-forming molecular recognition features with cross species sequence alignments | Q34708119 | ||
Identification and functions of usefully disordered proteins | Q34989882 | ||
Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders | Q35135581 | ||
Improving protein order-disorder classification using charge-hydropathy plots | Q35538193 | ||
Protein folding revisited. A polypeptide chain at the folding ? misfolding ? nonfolding cross-roads: which way to go? | Q35549177 | ||
C9ORF72 GGGGCC Expanded Repeats Produce Splicing Dysregulation which Correlates with Disease Severity in Amyotrophic Lateral Sclerosis | Q35643260 | ||
Clinical characteristics of patients with familial amyotrophic lateral sclerosis carrying the pathogenic GGGGCC hexanucleotide repeat expansion of C9ORF72. | Q35776923 | ||
ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. | Q35886826 | ||
Targeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: another illustration of the D(2) concept | Q36020398 | ||
Novel clinical associations with specific C9ORF72 transcripts in patients with repeat expansions in C9ORF72. | Q36304922 | ||
Structural analysis of disease-related TDP-43 D169G mutation: linking enhanced stability and caspase cleavage efficiency to protein accumulation | Q36588602 | ||
The neuropathology of FTD associated With ALS. | Q37036221 | ||
CDF it all: consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions | Q37195737 | ||
ALS mutant SOD1 interacts with G3BP1 and affects stress granule dynamics | Q37256571 | ||
Antisense transcripts of the expanded C9ORF72 hexanucleotide repeat form nuclear RNA foci and undergo repeat-associated non-ATG translation in c9FTD/ALS | Q37316045 | ||
C9orf72 frontotemporal lobar degeneration is characterised by frequent neuronal sense and antisense RNA foci. | Q37316053 | ||
ANCHOR: web server for predicting protein binding regions in disordered proteins. | Q37381486 | ||
RAN proteins and RNA foci from antisense transcripts in C9ORF72 ALS and frontotemporal dementia | Q37409251 | ||
Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: the TDP-43 diseases | Q37409270 | ||
Reduced C9orf72 protein levels in frontal cortex of amyotrophic lateral sclerosis and frontotemporal degeneration brain with the C9ORF72 hexanucleotide repeat expansion | Q37706316 | ||
Unusual biophysics of intrinsically disordered proteins | Q38069936 | ||
P433 | issue | 7 | |
P921 | main subject | amyotrophic lateral sclerosis | Q206901 |
P304 | page(s) | 1297-1318 | |
P577 | publication date | 2016-11-12 | |
P1433 | published in | Cellular and Molecular Life Sciences | Q5058352 |
P1476 | title | Intrinsic disorder in proteins involved in amyotrophic lateral sclerosis | |
P478 | volume | 74 |
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