about
Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes.A spring-loaded release mechanism regulates domain movement and catalysis in phosphoglycerate kinaseMechanism of folding chamber closure in a group II chaperoninRecognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solutionThe refined structure of functional unit h of keyhole limpet hemocyanin (KLH1-h) reveals disulfide bridgesStructure of myxovirus resistance protein a reveals intra- and intermolecular domain interactions required for the antiviral functionSymmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle.Remodeling of actin filaments by ADF/cofilin proteinsThe Crystal Structures of the Eukaryotic Chaperonin CCT Reveal Its Functional PartitioningApplication of DEN refinement and automated model building to a difficult case of molecular-replacement phasing: the structure of a putative succinyl-diaminopimelate desuccinylase from Corynebacterium glutamicumVisualizing GroEL/ES in the Act of Encapsulating a Folding ProteinFilaments from Ignicoccus hospitalis show diversity of packing in proteins containing N-terminal type IV pilin helices.Improving the Accuracy of Macromolecular Structure Refinement at 7 Å ResolutionLigand-induced structural changes in the cyclic nucleotide-modulated potassium channel MloK1.Energy barriers and driving forces in tRNA translocation through the ribosomeOutcome of the first electron microscopy validation task force meetingA grid-enabled web service for low-resolution crystal structure refinementSuper-resolution biomolecular crystallography with low-resolution dataArchaeal actin from a hyperthermophile forms a single-stranded filamentNear-atomic resolution for one state of F-actin.Structural polymorphism in F-actin.Deformable elastic network refinement for low-resolution macromolecular crystallography.Single-molecule fluorescence resonance energy transfer reveals a dynamic equilibrium between closed and open conformations of syntaxin 1.Combining efficient conformational sampling with a deformable elastic network model facilitates structure refinement at low resolution.Small-angle X-ray scattering of apolipoprotein A-IV reveals the importance of its termini for structural stability.Outcome of the First wwPDB Hybrid/Integrative Methods Task Force WorkshopHybrid methods for macromolecular structure determination: experiment with expectations.Improving the visualization of cryo-EM density reconstructions.Real-space refinement with DireX: from global fitting to side-chain improvements.Detecting protein-induced folding of the U4 snRNA kink-turn by single-molecule multiparameter FRET measurements.Simulation of fluorescence anisotropy experiments: probing protein dynamics.Fibril structure of amyloid-β(1-42) by cryo-electron microscopy.Branchpoint Expansion in a Fully Complementary Three-Way DNA JunctionGlobal Structure of Forked DNA in Solution Revealed by High-Resolution Single-Molecule FRETAtomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopyCryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils
P50
Q24339219-8E0052C4-0A3B-4A3E-9FBE-F29B8CE47FFFQ24614282-89DB3A82-D198-4A57-9116-397A1EC42B13Q24631877-11A939CB-9CDC-4450-A52C-62BC16DB91C1Q27650851-754FA310-71C0-4ECE-B29F-F3292028637FQ27667139-F4AF72EF-A999-4C92-B22A-D2FE0E4A742CQ27674633-40CAE959-5D28-4BD1-BA64-A1C5670E28B2Q27675341-A0FF8D08-6474-402A-9FA9-A2DC3D70FC46Q27676118-0209E4DF-55CC-43C4-9A8C-C348AA237468Q27676746-A3400D17-8D95-4DD2-A419-FBA808BB03DEQ27678525-BDB7C9D7-99E5-4C60-A335-01BE7B106351Q27678536-D044D57A-D6EF-4EF3-A7C3-606E285C227DQ27679443-CB32CF8C-4567-4C80-8BA3-6A054EC0D8A4Q27679554-AC3C3049-55E2-4B34-9E52-F58886977DF6Q27681473-FED8C637-259F-4E02-A73E-69158FEA4455Q27687431-23CFBE0F-2EE1-40E1-B330-D08C273C55DFQ28730539-98C1CC58-9915-4869-907E-317F9BE511EFQ28731934-ED31743A-4953-4B46-975C-9FE4BF5BE20AQ29616381-456E1611-C37E-43C1-B94A-C7C1A8D36F8EQ30279091-C601C497-185F-4E45-A5E0-6B72656E57B7Q30301084-F66D3840-89FF-454B-816B-F61AD6C6BE33Q30432555-05CBAC8E-46EA-43AC-8460-C61CF36C90A2Q34148076-3B60916F-B67B-4036-84A4-494651A6D474Q34788804-1B7078E2-E632-4496-A506-838910AD67BFQ36404096-A9FB899E-3E23-4EDD-B583-43B2BF22B6C1Q36620796-E218E316-FC05-4ED8-A5A9-C4CE10BC59F5Q37066138-7F946159-1BBD-46F8-AD47-2CABD99F8E12Q38385834-9CDDA4D3-54D5-47E5-A20A-286DD808A7B2Q41605053-6053767F-CF16-496B-A89C-071A0593EE71Q41613255-044B3498-C049-40C8-A254-26CC1AAADBCCQ42216577-1CB8A653-3DDB-4827-9948-9031A4A4DD6DQ43203268-746435A8-6973-4CE7-98E2-CFF11A050A2BQ47838176-7B3F72AF-2D6D-4A5B-918B-643406AB3670Q58043568-AD203B75-3D0E-4AA3-9FA2-46E09B056599Q58043586-D4EAFBB0-9E59-4A40-AFA5-C77E8C71F93AQ92757035-0C1AAED2-51DA-435A-A09F-B96D1FAD9C75Q96431669-588391F2-20A2-48B6-B9D0-34D1E0F6831B
P50
description
hulumtues
@sq
researcher
@en
ricercatore
@it
wetenschapper
@nl
հետազոտող
@hy
name
Gunnar F. Schröder
@ast
Gunnar F. Schröder
@en
Gunnar F. Schröder
@es
Gunnar F. Schröder
@nl
Gunnar F. Schröder
@sl
type
label
Gunnar F. Schröder
@ast
Gunnar F. Schröder
@en
Gunnar F. Schröder
@es
Gunnar F. Schröder
@nl
Gunnar F. Schröder
@sl
prefLabel
Gunnar F. Schröder
@ast
Gunnar F. Schröder
@en
Gunnar F. Schröder
@es
Gunnar F. Schröder
@nl
Gunnar F. Schröder
@sl
P214
P1053
H-5261-2013
P106
P1153
7102896562
P21
P214
P31
P3829
P496
0000-0003-1803-5431
P7859
viaf-47858212