126 related articles for article (PubMed ID: 21372082)
1. ncIDP-assign: a SPARKY extension for the effective NMR assignment of intrinsically disordered proteins.
Tamiola K; Mulder FA
Bioinformatics; 2011 Apr; 27(7):1039-40. PubMed ID: 21372082
[TBL] [Abstract][Full Text] [Related]
2. Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Wood K; Paz A; Dijkstra K; Scheek RM; Otten R; Silman I; Sussman JL; Mulder FA
Biomol NMR Assign; 2012 Apr; 6(1):15-8. PubMed ID: 21647611
[TBL] [Abstract][Full Text] [Related]
3. NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy.
Lee W; Tonelli M; Markley JL
Bioinformatics; 2015 Apr; 31(8):1325-7. PubMed ID: 25505092
[TBL] [Abstract][Full Text] [Related]
4. Conformational propensities of intrinsically disordered proteins from NMR chemical shifts.
Kragelj J; Ozenne V; Blackledge M; Jensen MR
Chemphyschem; 2013 Sep; 14(13):3034-45. PubMed ID: 23794453
[TBL] [Abstract][Full Text] [Related]
5. PISA-SPARKY: an interactive SPARKY plugin to analyze oriented solid-state NMR spectra of helical membrane proteins.
Weber DK; Wang S; Markley JL; Veglia G; Lee W
Bioinformatics; 2020 May; 36(9):2915-2916. PubMed ID: 31930377
[TBL] [Abstract][Full Text] [Related]
6. PINE-SPARKY: graphical interface for evaluating automated probabilistic peak assignments in protein NMR spectroscopy.
Lee W; Westler WM; Bahrami A; Eghbalnia HR; Markley JL
Bioinformatics; 2009 Aug; 25(16):2085-7. PubMed ID: 19497931
[TBL] [Abstract][Full Text] [Related]
7. An assignment of intrinsically disordered regions of proteins based on NMR structures.
Ota M; Koike R; Amemiya T; Tenno T; Romero PR; Hiroaki H; Dunker AK; Fukuchi S
J Struct Biol; 2013 Jan; 181(1):29-36. PubMed ID: 23142703
[TBL] [Abstract][Full Text] [Related]
8. Sequence-specific random coil chemical shifts of intrinsically disordered proteins.
Tamiola K; Acar B; Mulder FA
J Am Chem Soc; 2010 Dec; 132(51):18000-3. PubMed ID: 21128621
[TBL] [Abstract][Full Text] [Related]
9. Quantitative Protein Disorder Assessment Using NMR Chemical Shifts.
Nielsen JT; Mulder FAA
Methods Mol Biol; 2020; 2141():303-317. PubMed ID: 32696364
[TBL] [Abstract][Full Text] [Related]
10. NMR Spectroscopic Studies of the Conformational Ensembles of Intrinsically Disordered Proteins.
Kurzbach D; Kontaxis G; Coudevylle N; Konrat R
Adv Exp Med Biol; 2015; 870():149-85. PubMed ID: 26387102
[TBL] [Abstract][Full Text] [Related]
11. Speeding up sequence specific assignment of IDPs.
Bermel W; Bertini I; Felli IC; Gonnelli L; Koźmiński W; Piai A; Pierattelli R; Stanek J
J Biomol NMR; 2012 Aug; 53(4):293-301. PubMed ID: 22684679
[TBL] [Abstract][Full Text] [Related]
12. CHESPA/CHESCA-SPARKY: automated NMR data analysis plugins for SPARKY to map protein allostery.
Shao H; Boulton S; Olivieri C; Mohamed H; Akimoto M; Subrahmanian MV; Veglia G; Markley JL; Melacini G; Lee W
Bioinformatics; 2021 May; 37(8):1176-1177. PubMed ID: 32926121
[TBL] [Abstract][Full Text] [Related]
13. Linear discriminant analysis reveals hidden patterns in NMR chemical shifts of intrinsically disordered proteins.
Romero JA; Putko P; Urbańczyk M; Kazimierczuk K; Zawadzka-Kazimierczuk A
PLoS Comput Biol; 2022 Oct; 18(10):e1010258. PubMed ID: 36201530
[TBL] [Abstract][Full Text] [Related]
14. PINE-SPARKY.2 for automated NMR-based protein structure research.
Lee W; Markley JL
Bioinformatics; 2018 May; 34(9):1586-1588. PubMed ID: 29281006
[TBL] [Abstract][Full Text] [Related]
15. NMR probing and visualization of correlated structural fluctuations in intrinsically disordered proteins.
Kurzbach D; Beier A; Vanas A; Flamm AG; Platzer G; Schwarz TC; Konrat R
Phys Chem Chem Phys; 2017 Apr; 19(16):10651-10656. PubMed ID: 28397898
[TBL] [Abstract][Full Text] [Related]
16. High-dimensional NMR methods for intrinsically disordered proteins studies.
Grudziąż K; Zawadzka-Kazimierczuk A; Koźmiński W
Methods; 2018 Sep; 148():81-87. PubMed ID: 29705209
[TBL] [Abstract][Full Text] [Related]
17. Molecular Dynamics Simulations Combined with Nuclear Magnetic Resonance and/or Small-Angle X-ray Scattering Data for Characterizing Intrinsically Disordered Protein Conformational Ensembles.
Chan-Yao-Chong M; Durand D; Ha-Duong T
J Chem Inf Model; 2019 May; 59(5):1743-1758. PubMed ID: 30840442
[TBL] [Abstract][Full Text] [Related]
18. SCAssign: a sparky extension for the NMR resonance assignment of aliphatic side-chains of uniformly 13C,15N-labeled large proteins.
Zhang L; Yang D
Bioinformatics; 2006 Nov; 22(22):2833-4. PubMed ID: 16966359
[TBL] [Abstract][Full Text] [Related]
19. NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines.
Brutscher B; Felli IC; Gil-Caballero S; Hošek T; Kümmerle R; Piai A; Pierattelli R; Sólyom Z
Adv Exp Med Biol; 2015; 870():49-122. PubMed ID: 26387100
[TBL] [Abstract][Full Text] [Related]
20. Random coil chemical shifts for serine, threonine and tyrosine phosphorylation over a broad pH range.
Hendus-Altenburger R; Fernandes CB; Bugge K; Kunze MBA; Boomsma W; Kragelund BB
J Biomol NMR; 2019 Dec; 73(12):713-725. PubMed ID: 31598803
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
