Phosphorylation Increases Persistence Length and End-to-End Distance of a Segment of Tau Protein

scientific article

Phosphorylation Increases Persistence Length and End-to-End Distance of a Segment of Tau Protein is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1016/J.BPJ.2015.12.013
P932PMC publication ID4725354
P698PubMed publication ID26789759

P50authorTravis P SchrankQ96070025
P2093author name stringVincent J Hilser
W Austin Elam
Alexander F Chin
Dmitri Toptygin
P2860cites workThe structure and function of proline-rich regions in proteinsQ24528663
n-->pi* interactions in proteinsQ24632433
Calculation of protein extinction coefficients from amino acid sequence dataQ27861073
Extended disordered proteins: targeting function with less scaffoldQ28208096
Structural polymorphism of 441-residue tau at single residue resolutionQ28474834
The importance of intrinsic disorder for protein phosphorylationQ28776125
Comparative genomics of the eukaryotesQ29547504
Spectroscopic Determination of Tryptophan and Tyrosine in Proteins*Q29555850
Intrinsic disorder and protein functionQ29616415
Exploring the impact of polyproline II (PII) conformational bias on the binding of peptides to the SEM-5 SH3 domainQ30157656
An electronic effect on protein structure.Q30332873
Flexible nets. The roles of intrinsic disorder in protein interaction networks.Q30351593
Energetics of an n --> pi interaction that impacts protein structure.Q30357225
Contour length and refolding rate of a small protein controlled by engineered disulfide bonds.Q30357288
Melting of the left-handed helical conformation of charged poly-L-lysineQ72160886
Intrinsic protein disorder in complete genomesQ77145749
A Raman optical activity study of rheomorphism in caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteinsQ77470256
Thermodynamic mechanism and consequences of the polyproline II (PII) structural bias in the denatured states of proteinsQ80380288
The N-terminal module of HPV16 E7 is an intrinsically disordered domain that confers conformational and recognition plasticity to the oncoproteinQ80835837
The polyproline II conformation in short alanine peptides is noncooperativeQ30970632
Competition between intramolecular hydrogen bonds and solvation in phosphorylated peptides: simulations with explicit and implicit solventQ31049590
Residual structure in disordered peptides and unfolded proteins from multivariate analysis and ab initio simulation of Raman optical activity dataQ31122954
Effect of flexibility and cis residues in single-molecule FRET studies of polyprolineQ31137335
Statistical coil model of the unfolded state: resolving the reconciliation problemQ33222591
Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomesQ33252616
Conformational preferences and prolyl cis-trans isomerization of phosphorylated Ser/Thr-Pro motifsQ33514673
Polyproline and the "spectroscopic ruler" revisited with single-molecule fluorescence.Q33863222
Unusual compactness of a polyproline type II structureQ33920025
Polyproline II propensities from GGXGG peptides reveal an anticorrelation with beta-sheet scalesQ34212739
Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residuesQ34360837
Polyproline II conformation is one of many local conformational states and is not an overall conformation of unfolded peptides and proteins.Q34478711
Beyond the random coil: stochastic conformational switching in intrinsically disordered proteinsQ34786728
Polyproline II structure in proteins: identification by chiroptical spectroscopies, stability, and functionsQ34978349
Polymer models of protein stability, folding, and interactions.Q35673797
Conformational energy and configurational statistics of poly-L-prolineQ35971479
Stereoelectronic effects on polyproline conformationQ36457988
Reassessing random-coil statistics in unfolded proteinsQ37487200
Conformational stability of globular proteinsQ37809418
Abnormal hyperphosphorylation of tau: sites, regulation, and molecular mechanism of neurofibrillary degenerationQ38019803
Evolutionary conservation of the polyproline II conformation surrounding intrinsically disordered phosphorylation sitesQ38492530
OGlcNAcylation and phosphorylation have opposing structural effects in tau: phosphothreonine induces particular conformational orderQ39045088
Direct effects of phosphorylation on the preferred backbone conformation of peptides: a nuclear magnetic resonance studyQ40222599
Effect of Diffusion on Resonance Energy Transfer Rate Distributions: Implications for Distance MeasurementsQ40551995
Host-guest scale of left-handed polyproline II helix formation.Q40565690
Conservation of polyproline II helices in homologous proteins: implications for structure prediction by model buildingQ41869924
Resolution of the fluorescence excitation spectrum of indole into the 1La and 1Lb excitation bandsQ43613421
Tripeptides adopt stable structures in water. A combined polarized visible Raman, FTIR, and VCD spectroscopy studyQ44229856
Stable conformations of tripeptides in aqueous solution studied by UV circular dichroism spectroscopyQ44498802
The conformation of tetraalanine in water determined by polarized Raman, FT-IR, and VCD spectroscopyQ44783193
A strained DNA binding helix is conserved for site recognition, folding nucleation, and conformational modulation.Q45280412
Reconciling observations of sequence-specific conformational propensities with the generic polymeric behavior of denatured proteinsQ46662533
Scanning microcalorimetry and circular dichroism study of melting of the natural polypeptides in the left-handed helical conformation.Q48341659
Analysis of time-dependent red shifts in fluorescence emission from tryptophan residues in proteins.Q50484953
Hyperphosphorylation of tau induces local polyproline II helix.Q52570201
Temperature and urea have opposing impacts on polyproline II conformational bias.Q53113316
Role of phosphorylation in the conformation of tau peptides implicated in Alzheimer's disease.Q53342164
Tau protein isoforms, phosphorylation and role in neurodegenerative disorders11These authors contributed equally to this workQ57897029
Is polyproline II helix the killer conformation? a raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme 1 1Edited by A. R. FershtQ57909098
Microfluorometric analysis of protein thiol groups with a coumarinylphenylmaleimideQ71045514
Domains of tau protein and interactions with microtubulesQ72146653
P433issue2
P407language of work or nameEnglishQ1860
P304page(s)362-371
P577publication date2016-01-01
P1433published inBiophysical JournalQ2032955
P1476titlePhosphorylation Increases Persistence Length and End-to-End Distance of a Segment of Tau Protein
P478volume110

Reverse relations

cites work (P2860)
Q64984224Architectural Dynamics of CaMKII-Actin Networks.
Q47214435Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation
Q48094432Left-handed polyproline-II helix revisited: proteins causing proteopathies.
Q89149291N-terminal domain of human uracil DNA glycosylase (hUNG2) promotes targeting to uracil sites adjacent to ssDNA-dsDNA junctions
Q45408047Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation.
Q64287035The role of annealing and fragmentation in human tau aggregation dynamics

Search more.