TMDET: web server for detecting transmembrane regions of proteins by using their 3D coordinates

By Gábor E. Tusnády, Zsuzsanna Dosztányi, István Simon. 2005

152 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

How researchers see this paper

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

In Materials Chemistry

1. Jeffrey J. Gray
2. Sergey Lyskov
3. Julia Koehler Leman
4. Brian D. Weitzner
5. Amanda M. Duran
6. Richard Bonneau
7. Drew C. Tilley
8. Assaf Elazar

In Molecular Biology

1. Jeffrey J. Gray
2. Julia Koehler Leman
3. Sergey Lyskov
4. Brian D. Weitzner
5. Rebecca F. Alford
6. Mikhail A. Lomize
7. Henry I. Mosberg
8. Andrei L. Lomize

Citations in the corpus

• Computing structure-based lipid accessibility of membrane proteins with mp_lipid_acc in RosettaMP (2016, methodology): “Protein embedding in the membrane is therefore predicted using computational approaches that rely on different score functions, such as TMDET [10], PPM [11], and iMembrane [12].”
• OPM database and PPM web server: resources for positioning of proteins in membranes (2011, methodology): “Comparison of the PPM-server with other existing web servers for positioning of proteins in membranes, E Z (22), TMDET (23), MAPS (24) and MAPAS (16), demonstrates that PPM clearly outperforms all of them in scope and accuracy and represents the only server that correctly predicts membrane-binding s”
• An Integrated Framework Advancing Membrane Protein Modeling and Design (2015, methodology): “These values can be computed from PPM [42] or TMDET [41], two servers that transform membrane protein structures into membrane coordinates with the membrane center at z = 0 and membrane normal along the z-axis.”