670 related articles for article (PubMed ID: 18556554)
1. Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution.
Lange OF; Lakomek NA; Farès C; Schröder GF; Walter KF; Becker S; Meiler J; Grubmüller H; Griesinger C; de Groot BL
Science; 2008 Jun; 320(5882):1471-5. PubMed ID: 18556554
[TBL] [Abstract][Full Text] [Related]
2. Residual dipolar couplings as a tool to study molecular recognition of ubiquitin.
Lakomek NA; Lange OF; Walter KF; Farès C; Egger D; Lunkenheimer P; Meiler J; Grubmüller H; Becker S; de Groot BL; Griesinger C
Biochem Soc Trans; 2008 Dec; 36(Pt 6):1433-7. PubMed ID: 19021570
[TBL] [Abstract][Full Text] [Related]
3. Ensemble calculations of unstructured proteins constrained by RDC and PRE data: a case study of urea-denatured ubiquitin.
Huang JR; Grzesiek S
J Am Chem Soc; 2010 Jan; 132(2):694-705. PubMed ID: 20000836
[TBL] [Abstract][Full Text] [Related]
4. De novo determination of bond orientations and order parameters from residual dipolar couplings with high accuracy.
Briggman KB; Tolman JR
J Am Chem Soc; 2003 Aug; 125(34):10164-5. PubMed ID: 12926926
[TBL] [Abstract][Full Text] [Related]
5. Conformational and dynamic changes at the interface contribute to ligand binding by ubiquitin.
Sundd M
Biochemistry; 2012 Oct; 51(41):8111-24. PubMed ID: 23035694
[TBL] [Abstract][Full Text] [Related]
6. A correspondence between solution-state dynamics of an individual protein and the sequence and conformational diversity of its family.
Friedland GD; Lakomek NA; Griesinger C; Meiler J; Kortemme T
PLoS Comput Biol; 2009 May; 5(5):e1000393. PubMed ID: 19478996
[TBL] [Abstract][Full Text] [Related]
7. Anisotropic small amplitude Peptide plane dynamics in proteins from residual dipolar couplings.
Bernadó P; Blackledge M
J Am Chem Soc; 2004 Apr; 126(15):4907-20. PubMed ID: 15080696
[TBL] [Abstract][Full Text] [Related]
8. Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
van Dijk AD; Fushman D; Bonvin AM
Proteins; 2005 Aug; 60(3):367-81. PubMed ID: 15937902
[TBL] [Abstract][Full Text] [Related]
9. Conformational flexibility of a microcrystalline globular protein: order parameters by solid-state NMR spectroscopy.
Lorieau JL; McDermott AE
J Am Chem Soc; 2006 Sep; 128(35):11505-12. PubMed ID: 16939274
[TBL] [Abstract][Full Text] [Related]
10. Validation of X-ray Crystal Structure Ensemble Representations of SARS-CoV-2 Main Protease by Solution NMR Residual Dipolar Couplings.
Shen Y; Robertson AJ; Bax A
J Mol Biol; 2023 Jun; 435(11):168067. PubMed ID: 37330294
[TBL] [Abstract][Full Text] [Related]
11. Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: quantitative and absolute determination of backbone motion in ubiquitin.
Salmon L; Bouvignies G; Markwick P; Lakomek N; Showalter S; Li DW; Walter K; Griesinger C; Brüschweiler R; Blackledge M
Angew Chem Int Ed Engl; 2009; 48(23):4154-7. PubMed ID: 19415702
[TBL] [Abstract][Full Text] [Related]
12. Analysis of interdomain dynamics in a two-domain protein using residual dipolar couplings together with 15N relaxation data.
Ryabov Y; Fushman D
Magn Reson Chem; 2006 Jul; 44 Spec No():S143-51. PubMed ID: 16823894
[TBL] [Abstract][Full Text] [Related]
13. A hydrogen bond regulates slow motions in ubiquitin by modulating a β-turn flip.
Sidhu A; Surolia A; Robertson AD; Sundd M
J Mol Biol; 2011 Sep; 411(5):1037-48. PubMed ID: 21741979
[TBL] [Abstract][Full Text] [Related]
14. Weak alignment NMR: a hawk-eyed view of biomolecular structure.
Bax A; Grishaev A
Curr Opin Struct Biol; 2005 Oct; 15(5):563-70. PubMed ID: 16140525
[TBL] [Abstract][Full Text] [Related]
15. Picosecond to Millisecond Structural Dynamics in Human Ubiquitin.
Lindorff-Larsen K; Maragakis P; Piana S; Shaw DE
J Phys Chem B; 2016 Aug; 120(33):8313-20. PubMed ID: 27082121
[TBL] [Abstract][Full Text] [Related]
16. Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin.
Haller JD; Schanda P
J Biomol NMR; 2013 Nov; 57(3):263-80. PubMed ID: 24105432
[TBL] [Abstract][Full Text] [Related]
17. Conformational instability of the MARK3 UBA domain compromises ubiquitin recognition and promotes interaction with the adjacent kinase domain.
Murphy JM; Korzhnev DM; Ceccarelli DF; Briant DJ; Zarrine-Afsar A; Sicheri F; Kay LE; Pawson T
Proc Natl Acad Sci U S A; 2007 Sep; 104(36):14336-41. PubMed ID: 17726107
[TBL] [Abstract][Full Text] [Related]
18. Nuclear magnetic resonance provides a quantitative description of protein conformational flexibility on physiologically important time scales.
Salmon L; Bouvignies G; Markwick P; Blackledge M
Biochemistry; 2011 Apr; 50(14):2735-47. PubMed ID: 21388216
[TBL] [Abstract][Full Text] [Related]
19. How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation?
Clore GM; Schwieters CD
J Am Chem Soc; 2004 Mar; 126(9):2923-38. PubMed ID: 14995210
[TBL] [Abstract][Full Text] [Related]
20. The structure of cyclolinopeptide A in chloroform refined by RDC measurements.
Huben K; Jewgiński M; Pabis A; Paluch P; Luy B; Jankowski S
J Pept Sci; 2014 Nov; 20(11):901-7. PubMed ID: 25111589
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
