Crystal Structure of Rhodopsin: A G‐Protein‐Coupled Receptor
By R. Stenkamp, D. Teller, Krzysztof Palczewski. ChemBioChem, 2002
4,572 citations recorded by the source corpus.
Subfields: Cellular and Molecular Neuroscience, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/a4ffdf18203baa73a983a2a3dc0b6adbe764c72a
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Cellular and Molecular Neuroscience
- Brian K. Kobilka
- David E. Gloriam
- Raymond C. Stevens
- Vadim Cherezov
- Vsevolod Katritch
- Ye Fang
- Vignir Ísberg
- Arthur Christopoulos
In Molecular Biology
- Brian K. Kobilka
- David E. Gloriam
- Vsevolod Katritch
- Raymond C. Stevens
- Ye Fang
- Brian K. Shoichet
- Vadim Cherezov
- John J. Irwin
Citations in the corpus
- Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions (2012, background): “53 (18) to slightly less than the diameter of one water molecule (2.”
- Evolutionarily conserved networks of residues mediate allosteric communication in proteins (2003, neutral): “For example, Phe293, Leu294, Ala295, Ala299 and Phe91 in rhodopsin make intra- and interhelical packing interactions with position 296, and Glu113 makes a salt-bridge interaction with the protonated form of the Schiff bas”
- International Union of Pharmacology. XLV. Classification of the Kinin Receptor Family: from Molecular Mechanisms to Pathophysiological Consequences (2005, background): “Notably, cysteine in EL-2 and EL-3 are conserved in most members of the GPCR superfamily, and the crystal structure of rhodopsin has revealed that they form a disulfide loop which most likely stabilizes the correctly folded conformation of the receptor (Palczewski et al., 2000).”
- How the olfactory system makes sense of scents (2001, background): “), and in common with the binding site of retinal in rhodopsi”
- Multipass membrane protein structure prediction using Rosetta (2005, neutral): “…two-helix proteins generated best models with RMSD values ranging from 3.6 to 6.5 Å. 70 For example, using these data, Baldwin et al., 67 Fleishman et al., 69 and Beuming and Weinstein 70 constructed models of rhodopsin with RMSDs of 3.2, 3.7, and 3.0 Å to the native structure, 71,72 respectively.”
- Structure of bovine rhodopsin in a trigonal crystal form. (2003, methodology): “Here we describe the refined structure of bovine rhodopsin in the trigonal crystal form, and compare it with previous structural reports of the tetragonal crystal form.(14,18,19) In addition, we relate the crystal structures to the membrane environment by docking them into a cryo-EM map(10) of 2D cr”