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Helical defects in microRNA influence protein binding by TAR RNA binding proteinValidation of Molecular Dynamics Simulations of Biomolecules Using NMR Spin Relaxation as Benchmarks: Application to the AMBER99SB Force Field.Structural heterogeneity in the intrinsically disordered RNA polymerase II C-terminal domain.Phosphorylation induces sequence-specific conformational switches in the RNA polymerase II C-terminal domain.Expanding the proteome of an RNA virus by phosphorylation of an intrinsically disordered viral protein.Correlated motions in the U1 snRNA stem/loop 2:U1A RBD1 complex.The role of human Dicer-dsRBD in processing small regulatory RNAsDeformability in the cleavage site of primary microRNA is not sensed by the double-stranded RNA binding domains in the microprocessor component DGCR8Ensemble analysis of primary microRNA structure reveals an extensive capacity to deform near the Drosha cleavage site.Binding by TRBP-dsRBD2 Does Not Induce Bending of Double-Stranded RNA.Structure and dynamics of Ca2+-binding domain 1 of the Na+/Ca2+ exchanger in the presence and in the absence of Ca2+Quantitative biophysical characterization of intrinsically disordered proteins.Application of NMR to studies of intrinsically disordered proteins.A High-Throughput Biological Calorimetry Core: Steps to Startup, Run, and Maintain a Multiuser Facility.Assessing Coupled Protein Folding and Binding Through Temperature-Dependent Isothermal Titration Calorimetry.Carbon-Detected (15)N NMR Spin Relaxation of an Intrinsically Disordered Protein: FCP1 Dynamics Unbound and in Complex with RAP74.Engineering double-stranded RNA binding activity into the Drosha double-stranded RNA binding domain results in a loss of microRNA processing function.Generating NMR chemical shift assignments of intrinsically disordered proteins using carbon-detected NMR methods.Quantitative lid dynamics of MDM2 reveals differential ligand binding modes of the p53-binding cleft.MD simulations of the dsRBP DGCR8 reveal correlated motions that may aid pri-miRNA binding.Dynamic origins of differential RNA binding function in two dsRBDs from the miRNA "microprocessor" complex.Altering the RNA-binding mode of the U1A RBD1 protein.Role of Ordered Proteins in the Folding-Upon-Binding of Intrinsically Disordered Proteins.Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: quantitative and absolute determination of backbone motion in ubiquitin.Iron responsive element RNA flexibility described by NMR and isotropic reorientational eigenmode dynamics.Incorporating 1H chemical shift determination into 13C-direct detected spectroscopy of intrinsically disordered proteins in solution.A functional role for correlated motion in the N-terminal RNA-binding domain of human U1A protein.The disordered C-terminus of the RNA polymerase II phosphatase FCP1 is partially helical in the unbound state.Atomistic simulations reveal structural disorder in the RAP74-FCP1 complex.NMR assignment of the intrinsically disordered C-terminal region of Homo sapiens FCP1 in the unbound state.Structural basis for rare earth element recognition by Methylobacterium extorquens lanmodulinNative-Based Simulations of the Binding Interaction Between RAP74 and the Disordered FCP1 PeptideEntropy Localization in ProteinsStructural dynamics of protein backbone φ angles: extended molecular dynamics simulations versus experimental 3 J scalar couplingsA Multifaceted Approach to the Interpretation of NMR Order Parameters: A Case Study of a Dynamic α-Helix†Quantitative Molecular Ensemble Interpretation of NMR Dipolar Couplings without RestraintsToward Quantitative Interpretation of Methyl Side-Chain Dynamics from NMR by Molecular Dynamics SimulationsUltrasound-Guided Cytosolic Protein Delivery via Transient Fluorous MasksSolution Ensemble of the C-Terminal Domain from the Transcription Factor Pdx1 Resembles an Excluded Volume Polymer
P50
Q24315828-B9735902-E199-4A34-AE7F-62F0DBB99697Q31029830-9C9CF180-2DC7-4699-95B0-F19BEFD3070CQ33705692-2191587B-00F3-431F-8C99-3DC4914340B5Q33705708-06FE4D9B-2949-4DAB-8EBF-2B67C9CA4836Q34107289-4D41358B-EDA8-4D69-B547-C0C9ACBB7B6FQ34351208-A7341530-6283-4E5A-AE2E-DB746742053AQ34525711-32860381-A753-49B4-B72F-972A67CC2957Q35655524-7B743BBF-6A61-49F2-A97C-86AAFA0FE405Q36589329-641D319A-4FE9-4CE3-8062-68EA85B02CF6Q37034324-0900547B-A126-4FED-85E1-FC321986A717Q37243184-2E99254F-7850-4490-8D1C-2CC74F2BA16EQ38335959-A7C21608-169A-40BC-87DC-B0829E369887Q38684152-F0773E3B-7983-452E-B5D6-01921EFB3F26Q40078715-4FA9B488-3C4F-427D-8A66-3C945353B045Q40078777-D20C5129-6E91-47C8-9C27-E7B1D5DBC940Q40628866-545F735E-5C72-4BD3-9457-B68F0B1E61D6Q41323902-4529486F-E8AC-4479-A48E-9C8B52DCD480Q42004836-FCF22F1D-1E84-4E31-83FD-DE737DC9D0AAQ42653185-D7F60746-C0FF-4144-8551-D4D3A9CDA17BQ42739644-5AD66DEF-FC5A-432E-A185-8BD431EC3A1CQ43181153-44F7E200-D043-48DA-9232-24D337365AC5Q44691246-37FB6F99-F798-432C-82B6-414D206692E8Q47793430-D7817A2F-1CA5-4FA0-815E-9C122D48D8B8Q47881629-BE2A0661-5937-4243-80E6-E84B103D1602Q50756479-9CF5818C-988A-45A9-8903-33D9F3FF99FBQ51806670-AFAE18E5-73AF-4B07-86E4-CCBE111D9E78Q52032854-FDD0FFBC-90FA-486D-86FA-6391A30A7651Q53085411-7E3D59CE-1729-4361-9558-802F998D4870Q53402788-B3019889-F603-428B-805C-3F6DE4C2CD38Q53491673-BD86967F-9ED2-4120-BB1E-47E6A0E8CE22Q57795712-0A06A2F1-9504-4DB5-8A71-6380655117E6Q58622214-2AF68DA6-EDF3-402C-86A6-7C8B6A96C889Q58622225-F462573E-86F4-47B0-8A41-D0CA73A63BECQ58622233-45872E40-70F5-45F2-8D77-19B553165156Q58622235-E153D0A0-45AC-4AE8-99FB-84AC1B9994B9Q58622240-7F4EA3FF-0E28-4AAB-892D-E5027D0EB073Q58622242-41EA2AB4-D2BC-41C7-97B5-66477910E353Q90063644-11DDB3F5-4E18-4A6A-8479-30A18730E1A0Q90331357-CC18FD67-96F8-4BBC-A261-9182ABCCBF31
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Scott A Showalter
@ast
Scott A Showalter
@en
Scott A Showalter
@es
Scott A Showalter
@nl
Scott A Showalter
@sl
type
label
Scott A Showalter
@ast
Scott A Showalter
@en
Scott A Showalter
@es
Scott A Showalter
@nl
Scott A Showalter
@sl
prefLabel
Scott A Showalter
@ast
Scott A Showalter
@en
Scott A Showalter
@es
Scott A Showalter
@nl
Scott A Showalter
@sl
P1053
A-1655-2012
P106
P21
P31
P3829
P496
0000-0001-5179-032X