Three-dimensional protein fold determination from backbone amide pseudocontact shifts generated by lanthanide tags at multiple sites.

By H. Yagi, K. B. Pilla, A. Maleckis, B. Graham, Thomas Huber, G. Otting. 2013

78 citations recorded by the source corpus.

Subfields: Molecular Biology, Spectroscopy

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Santrupti Nerli
2. Nikolaos G. Sgourakis
3. K. B. Pilla
4. Julia Koehler Leman
5. Richard Bonneau
6. Thomas Huber
7. G. Otting
8. Georg Kuenze

In Spectroscopy

1. Santrupti Nerli
2. Nikolaos G. Sgourakis
3. Richard Bonneau
4. Thomas Huber
5. Jens Meiler
6. Julia Koehler Leman
7. Georg Kuenze
8. K. B. Pilla

Citations in the corpus

• CS-ROSETTA (2018, methodology): “PCS measurements can be combined with Abrelax to model protein structures with increased accuracy (Schmitz et al., 2012; Yagi et al., 2013).”
• Pseudocontact Shift-Driven Iterative Resampling for 3D Structure Determinations of Large Proteins. (2016, methodology): “4 4920 [21] C (OmpX) 2M06 148 6.”
• Integrative protein modeling in RosettaNMR from sparse paramagnetic restraints (2019, methodology): “This approach was extended for PCSs from multiple tagging sites and applied to the solution structure of ERp29, which uncovered flaws in a previous NOE-derived NMR structure (Yagi et al., 2013).”