
OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!
If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.
Requested Article:
Structured and disordered facets of the GPCR fold
AJ Venkatakrishnan, Tilman Flock, Daniel Estévez Prado, et al.
Current Opinion in Structural Biology (2014) Vol. 27, pp. 129-137
Closed Access | Times Cited: 79
AJ Venkatakrishnan, Tilman Flock, Daniel Estévez Prado, et al.
Current Opinion in Structural Biology (2014) Vol. 27, pp. 129-137
Closed Access | Times Cited: 79
Showing 1-25 of 79 citing articles:
GPCR Dynamics: Structures in Motion
Naomi R. Latorraca, AJ Venkatakrishnan, Ron O. Dror
Chemical Reviews (2016) Vol. 117, Iss. 1, pp. 139-155
Open Access | Times Cited: 674
Naomi R. Latorraca, AJ Venkatakrishnan, Ron O. Dror
Chemical Reviews (2016) Vol. 117, Iss. 1, pp. 139-155
Open Access | Times Cited: 674
Mechanisms of signalling and biased agonism in G protein-coupled receptors
Denise Wootten, Arthur Christopoulos, Maria Martí-Solano, et al.
Nature Reviews Molecular Cell Biology (2018) Vol. 19, Iss. 10, pp. 638-653
Open Access | Times Cited: 584
Denise Wootten, Arthur Christopoulos, Maria Martí-Solano, et al.
Nature Reviews Molecular Cell Biology (2018) Vol. 19, Iss. 10, pp. 638-653
Open Access | Times Cited: 584
Pharmacogenomics of GPCR Drug Targets
Alexander S. Hauser, Sreenivas Chavali, Ikuo Masuho, et al.
Cell (2017) Vol. 172, Iss. 1-2, pp. 41-54.e19
Open Access | Times Cited: 564
Alexander S. Hauser, Sreenivas Chavali, Ikuo Masuho, et al.
Cell (2017) Vol. 172, Iss. 1-2, pp. 41-54.e19
Open Access | Times Cited: 564
Illuminating G-Protein-Coupling Selectivity of GPCRs
Asuka Inoue, Francesco Raimondi, Francois Marie Ngako Kadji, et al.
Cell (2019) Vol. 177, Iss. 7, pp. 1933-1947.e25
Open Access | Times Cited: 533
Asuka Inoue, Francesco Raimondi, Francois Marie Ngako Kadji, et al.
Cell (2019) Vol. 177, Iss. 7, pp. 1933-1947.e25
Open Access | Times Cited: 533
The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease
M. Madan Babu
Biochemical Society Transactions (2016) Vol. 44, Iss. 5, pp. 1185-1200
Open Access | Times Cited: 357
M. Madan Babu
Biochemical Society Transactions (2016) Vol. 44, Iss. 5, pp. 1185-1200
Open Access | Times Cited: 357
Diverse activation pathways in class A GPCRs converge near the G-protein-coupling region
AJ Venkatakrishnan, Xavier Deupí, Guillaume Lebon, et al.
Nature (2016) Vol. 536, Iss. 7617, pp. 484-487
Open Access | Times Cited: 293
AJ Venkatakrishnan, Xavier Deupí, Guillaume Lebon, et al.
Nature (2016) Vol. 536, Iss. 7617, pp. 484-487
Open Access | Times Cited: 293
GPCR drug discovery: integrating solution NMR data with crystal and cryo-EM structures
Ichio Shimada, Takumi Ueda, Yutaka Kofuku, et al.
Nature Reviews Drug Discovery (2018) Vol. 18, Iss. 1, pp. 59-82
Open Access | Times Cited: 217
Ichio Shimada, Takumi Ueda, Yutaka Kofuku, et al.
Nature Reviews Drug Discovery (2018) Vol. 18, Iss. 1, pp. 59-82
Open Access | Times Cited: 217
Autoregulation of GPCR signalling through the third intracellular loop
Fredrik Sadler, Ning Ma, Michael Ritt, et al.
Nature (2023) Vol. 615, Iss. 7953, pp. 734-741
Open Access | Times Cited: 57
Fredrik Sadler, Ning Ma, Michael Ritt, et al.
Nature (2023) Vol. 615, Iss. 7953, pp. 734-741
Open Access | Times Cited: 57
Synergy between intrinsically disordered domains and structured proteins amplifies membrane curvature sensing
Wade F. Zeno, Upayan Baul, Wilton T. Snead, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 124
Wade F. Zeno, Upayan Baul, Wilton T. Snead, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 124
New Binding Sites, New Opportunities for GPCR Drug Discovery
H. C. Stephen Chan, Yi Li, Thamani Dahoun, et al.
Trends in Biochemical Sciences (2019) Vol. 44, Iss. 4, pp. 312-330
Open Access | Times Cited: 123
H. C. Stephen Chan, Yi Li, Thamani Dahoun, et al.
Trends in Biochemical Sciences (2019) Vol. 44, Iss. 4, pp. 312-330
Open Access | Times Cited: 123
Combinatorial expression of GPCR isoforms affects signalling and drug responses
Maria Martí-Solano, Stephanie E. Crilly, Duccio Malinverni, et al.
Nature (2020) Vol. 587, Iss. 7835, pp. 650-656
Open Access | Times Cited: 112
Maria Martí-Solano, Stephanie E. Crilly, Duccio Malinverni, et al.
Nature (2020) Vol. 587, Iss. 7835, pp. 650-656
Open Access | Times Cited: 112
An update on the physiological and therapeutic relevance of GPCR oligomers
Batoul Farran
Pharmacological Research (2017) Vol. 117, pp. 303-327
Closed Access | Times Cited: 106
Batoul Farran
Pharmacological Research (2017) Vol. 117, pp. 303-327
Closed Access | Times Cited: 106
Intrinsically Disordered Proteins Link Alternative Splicing and Post-translational Modifications to Complex Cell Signaling and Regulation
Jianhong Zhou, Suwen Zhao, A. Keith Dunker
Journal of Molecular Biology (2018) Vol. 430, Iss. 16, pp. 2342-2359
Open Access | Times Cited: 88
Jianhong Zhou, Suwen Zhao, A. Keith Dunker
Journal of Molecular Biology (2018) Vol. 430, Iss. 16, pp. 2342-2359
Open Access | Times Cited: 88
Structure-Based Sequence Alignment of the Transmembrane Domains of All Human GPCRs: Phylogenetic, Structural and Functional Implications
Vaclav Cvicek, William A. Goddard, Ravinder Abrol
PLoS Computational Biology (2016) Vol. 12, Iss. 3, pp. e1004805-e1004805
Open Access | Times Cited: 87
Vaclav Cvicek, William A. Goddard, Ravinder Abrol
PLoS Computational Biology (2016) Vol. 12, Iss. 3, pp. e1004805-e1004805
Open Access | Times Cited: 87
How phosphorylation impacts intrinsically disordered proteins and their function
Estella A. Newcombe, Elise Delaforge, Rasmus Hartmann‐Petersen, et al.
Essays in Biochemistry (2022) Vol. 66, Iss. 7, pp. 901-913
Open Access | Times Cited: 46
Estella A. Newcombe, Elise Delaforge, Rasmus Hartmann‐Petersen, et al.
Essays in Biochemistry (2022) Vol. 66, Iss. 7, pp. 901-913
Open Access | Times Cited: 46
Intrinsically disordered proteins and proteins with intrinsically disordered regions in neurodegenerative diseases
Orkid Coskuner‐Weber, Ozan Mirzanli, Vladimir N. Uversky
Biophysical Reviews (2022) Vol. 14, Iss. 3, pp. 679-707
Open Access | Times Cited: 45
Orkid Coskuner‐Weber, Ozan Mirzanli, Vladimir N. Uversky
Biophysical Reviews (2022) Vol. 14, Iss. 3, pp. 679-707
Open Access | Times Cited: 45
Function and dynamics of the intrinsically disordered carboxyl terminus of β2 adrenergic receptor
Jie Heng, Yunfei Hu, Guillermo Pérez‐Hernández, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 29
Jie Heng, Yunfei Hu, Guillermo Pérez‐Hernández, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 29
GPCRs involved in metabolic diseases: pharmacotherapeutic development updates
Hongchuan Jin, Hui Chen, Li Xie, et al.
Acta Pharmacologica Sinica (2024) Vol. 45, Iss. 7, pp. 1321-1336
Closed Access | Times Cited: 11
Hongchuan Jin, Hui Chen, Li Xie, et al.
Acta Pharmacologica Sinica (2024) Vol. 45, Iss. 7, pp. 1321-1336
Closed Access | Times Cited: 11
Comparing Class A GPCRs to bitter taste receptors
Antonella Di Pizio, Anat Levit, Michal Slutzki, et al.
Methods in cell biology (2015), pp. 401-427
Closed Access | Times Cited: 83
Antonella Di Pizio, Anat Levit, Michal Slutzki, et al.
Methods in cell biology (2015), pp. 401-427
Closed Access | Times Cited: 83
Phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR
Yutaro Shiraishi, Mei Natsume, Yutaka Kofuku, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 72
Yutaro Shiraishi, Mei Natsume, Yutaka Kofuku, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 72
Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit
Ching‐Ju Tsai, Jacopo Marino, Ricardo Adaixo, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 61
Ching‐Ju Tsai, Jacopo Marino, Ricardo Adaixo, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 61
Multi-functionality of proteins involved in GPCR and G protein signaling: making sense of structure–function continuum with intrinsic disorder-based proteoforms
Alexander V. Fonin, April L. Darling, Irina М. Kuznetsova, et al.
Cellular and Molecular Life Sciences (2019) Vol. 76, Iss. 22, pp. 4461-4492
Closed Access | Times Cited: 60
Alexander V. Fonin, April L. Darling, Irina М. Kuznetsova, et al.
Cellular and Molecular Life Sciences (2019) Vol. 76, Iss. 22, pp. 4461-4492
Closed Access | Times Cited: 60
Differential Regulation of GPCRs—Are GRK Expression Levels the Key?
Edda S. F. Matthees, Raphael S. Haider, Carsten Hoffmann, et al.
Frontiers in Cell and Developmental Biology (2021) Vol. 9
Open Access | Times Cited: 45
Edda S. F. Matthees, Raphael S. Haider, Carsten Hoffmann, et al.
Frontiers in Cell and Developmental Biology (2021) Vol. 9
Open Access | Times Cited: 45
Classification Model for the Second Extracellular Loop of Class A GPCRs
Alessandro Nicoli, Andreas Dunkel, Toni Giorgino, et al.
Journal of Chemical Information and Modeling (2022) Vol. 62, Iss. 3, pp. 511-522
Closed Access | Times Cited: 31
Alessandro Nicoli, Andreas Dunkel, Toni Giorgino, et al.
Journal of Chemical Information and Modeling (2022) Vol. 62, Iss. 3, pp. 511-522
Closed Access | Times Cited: 31
How do disordered regions achieve comparable functions to structured domains?
Natasha S. Latysheva, Tilman Flock, Robert J. Weatheritt, et al.
Protein Science (2015) Vol. 24, Iss. 6, pp. 909-922
Open Access | Times Cited: 51
Natasha S. Latysheva, Tilman Flock, Robert J. Weatheritt, et al.
Protein Science (2015) Vol. 24, Iss. 6, pp. 909-922
Open Access | Times Cited: 51