The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
Structural basis for chemokine recognition and activation of a viral G protein–coupled receptor
Open accessAbstract
Molecular “go” signals reveal their secrets: Chemokines are proteins that direct how cells move within the body. For instance, chemokines help immune cells locate invading pathogens and ensure that cells position themselves correctly within a developing organ. Cells detect chemokines through G protein–coupled receptors on their surface; however, the molecular details of how these proteins interact remain unclear (see the Perspective by Standfuss). Qin et al. solved the crystal structure of the chemokine receptor CXCR4 bound to the viral chemokine vMIP-II. Burg et al. solved the crystal structure of a viral chemokine receptor bound to the chemokine domain of CX3CL1. Given the role of chemokines in a number of diseases, these results may help in future drug design. Science , this issue p. 1117 , p. 1113 ; see also p. 1071
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
The CCP4 suite: programs for protein crystallography
Collaborative Computational Project, N. 4. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,270
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins
MacKerell, A. D., Bashford, D., Bellott, M., Dunbrack, R. L., Evanseck, J. D., Field, M. J., Fischer, S., Gao, J., Guo, H., Ha, S., et al. (1998) · The Journal of Physical Chemistry B · doi:10.1021/jp973084f · Cited by 14,311
MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
Inference of Macromolecular Assemblies from Crystalline State
Krissinel, E., & Henrick, K. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.022 · Cited by 9,984
CHARMM‐GUI: A web‐based graphical user interface for CHARMM
Jo, S., Kim, T., Iyer, V. G., & Im, W. (2008) · Journal of Computational Chemistry · doi:10.1002/jcc.20945 · Cited by 9,284
CHARMM: The biomolecular simulation program
Brooks, B. R., Brooks, C. L., Mackerell, A. D., Nilsson, L., Petrella, R. J., Roux, B., Won, Y., Archontis, G., Bartels, C., Boresch, S., et al. (2009) · Journal of Computational Chemistry · doi:10.1002/jcc.21287 · Cited by 8,939
Vanommeslaeghe, K., Hatcher, E., Acharya, C., Kundu, S., Zhong, S., Shim, J., Darian, E., Guvench, O., Lopes, P., Vorobyov, I., et al. (2010) · Journal of Computational Chemistry · doi:10.1002/jcc.21367 · Cited by 7,509
Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor
Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Trong, I. L., Teller, D. C., Okada, T., Stenkamp, R. E., et al. (2000) · Science · doi:10.1126/science.289.5480.739 · Cited by 5,637
Towards automated crystallographic structure refinement with phenix.refine
Afonine, P. V., Grosse-Kunstleve, R. W., Echols, N., Headd, J. J., Moriarty, N. W., Mustyakimov, M., Terwilliger, T. C., Urzhumtsev, A., Zwart, P. H., & Adams, P. D. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444912001308 · Cited by 5,511
Best, R. B., Zhu, X., Shim, J., Lopes, P. E. M., Mittal, J., Feig, M., & MacKerell, A. D. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct300400x · Cited by 4,532
Salomon-Ferrer, R., Götz, A. W., Poole, D., Le Grand, S., & Walker, R. C. (2013) · Journal of Chemical Theory and Computation · doi:10.1021/ct400314y · Cited by 3,372
Mackerell, A. D., Feig, M., & Brooks, C. L. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20065 · Cited by 3,319
Crystal structure of the β2 adrenergic receptor–Gs protein complex
Rasmussen, S. G. F., DeVree, B. T., Zou, Y., Kruse, A. C., Chung, K. Y., Kobilka, T. S., Thian, F. S., Chae, P. S., Pardon, E., Calinski, D., et al. (2011) · Nature · doi:10.1038/nature10361 · Cited by 3,009
Ballesteros, J. A., & Weinstein, H. (1995) · Methods in Neurosciences · doi:10.1016/s1043-9471(05)80049-7 · Cited by 2,999
CHARMM-GUI Membrane Builder toward realistic biological membrane simulations
Wu, E. L., Cheng, X., Jo, S., Rui, H., Song, K. C., Dávila-Contreras, E. M., Qi, Y., Lee, J., Monje-Galvan, V., Venable, R. M., et al. (2014) · Journal of Computational Chemistry · doi:10.1002/jcc.23702 · Cited by 2,656
The structure and function of G-protein-coupled receptors
Rosenbaum, D. M., Rasmussen, S. G. F., & Kobilka, B. K. (2009) · Nature · doi:10.1038/nature08144 · Cited by 2,534
The many roles of chemokines and chemokine receptors in inflammation
Charo, I. F., & Ransohoff, R. M. (2006) · New England Journal of Medicine · doi:10.1056/nejmra052723 · Cited by 2,523
A new class of membrane-bound chemokine with a CX3C motif
Bazan, J. F., Bacon, K. B., Hardiman, G., Wang, W., Soo, K., Rossi, D., Greaves, D. R., Zlotnik, A., & Schall, T. J. (1997) · Nature · doi:10.1038/385640a0 · Cited by 2,013
Structures of the CXCR4 Chemokine GPCR with Small-Molecule and Cyclic Peptide Antagonists
Wu, B., Chien, E. Y. T., Mol, C. D., Fenalti, G., Liu, W., Katritch, V., Abagyan, R., Brooun, A., Wells, P., Bi, F. C., et al. (2010) · Science · doi:10.1126/science.1194396 · Cited by 1,782
Molecular signatures of G-protein-coupled receptors
Venkatakrishnan, A. J., Deupi, X., Lebon, G., Tate, C. G., Schertler, G. F., & Babu, M. M. (2013) · Nature · doi:10.1038/nature11896 · Cited by 1,497
Self-citationOptimal description of a protein structure in terms of multiple groups undergoing TLS motion
Painter, J., & Merritt, E. A. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906005270 · Cited by 1,240
Automated Builder and Database of Protein/Membrane Complexes for Molecular Dynamics Simulations
Jo, S., Kim, T., & Im, W. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000880 · Cited by 1,216
OPM: Orientations of Proteins in Membranes database
Lomize, M. A., Lomize, A. L., Pogozheva, I. D., & Mosberg, H. I. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btk023 · Cited by 1,173
Collaboration gets the most out of software
Morin, A., Eisenbraun, B., Key, J., Sanschagrin, P. C., Timony, M. A., Ottaviano, M., & Sliz, P. (2013) · eLife · doi:10.7554/elife.01456 · Cited by 1,081
Le Grand, S., Götz, A. W., & Walker, R. C. (2013) · Computer Physics Communications · doi:10.1016/j.cpc.2012.09.022 · Cited by 1,075
GPCRdb: an information system for G protein-coupled receptors
Isberg, V., Mordalski, S., Munk, C., Rataj, K., Harpsøe, K., Hauser, A. S., Vroling, B., Bojarski, A. J., Vriend, G., & Gloriam, D. E. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1178 · Cited by 1,072
Structure-Function of the G Protein–Coupled Receptor Superfamily
Katritch, V., Cherezov, V., & Stevens, R. C. (2013) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-032112-135923 · Cited by 1,054
Isolating and engineering human antibodies using yeast surface display
Chao, G., Lau, W. L., Hackel, B. J., Sazinsky, S. L., Lippow, S. M., & Wittrup, K. D. (2006) · Nature Protocols · doi:10.1038/nprot.2006.94 · Cited by 909
TLSMD web server for the generation of multi-group TLS models
Painter, J., & Merritt, E. A. (2006) · Journal of Applied Crystallography · doi:10.1107/s0021889805038987 · Cited by 756
Chemokine receptors: multifaceted therapeutic targets
Proudfoot, A. E. I. (2002) · Nature Reviews Immunology · doi:10.1038/nri722 · Cited by 752
Structure of the CCR5 Chemokine Receptor–HIV Entry Inhibitor Maraviroc Complex
Tan, Q., Zhu, Y., Li, J., Chen, Z., Han, G. W., Kufareva, I., Li, T., Ma, L., Fenalti, G., Li, J., et al. (2013) · Science · doi:10.1126/science.1241475 · Cited by 712
Crystallizing membrane proteins using lipidic mesophases
Caffrey, M., & Cherezov, V. (2009) · Nature Protocols · doi:10.1038/nprot.2009.31 · Cited by 670
Activation mechanism of the β2-adrenergic receptor
Dror, R. O., Arlow, D. H., Maragakis, P., Mildorf, T. J., Pan, A. C., Xu, H., Borhani, D. W., & Shaw, D. E. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110499108 · Cited by 623
Self-citationAdrenaline-activated structure of β2-adrenoceptor stabilized by an engineered nanobody
Ring, A. M., Manglik, A., Kruse, A. C., Enos, M. D., Weis, W. I., Garcia, K. C., & Kobilka, B. K. (2013) · Nature · doi:10.1038/nature12572 · Cited by 491
Self-citationThe structural basis of agonist-induced activation in constitutively active rhodopsin
Standfuss, J., Edwards, P. C., D’Antona, A., Fransen, M., Xie, G., Oprian, D. D., & Schertler, G. F. X. (2011) · Nature · doi:10.1038/nature09795 · Cited by 476
Structural basis for modulation of a G-protein-coupled receptor by allosteric drugs
Dror, R. O., Green, H. F., Valant, C., Borhani, D. W., Valcourt, J. R., Pan, A. C., Arlow, D. H., Canals, M., Lane, J. R., Rahmani, R., et al. (2013) · Nature · doi:10.1038/nature12595 · Cited by 411
Self-citationStructural Basis of CXCR4 Sulfotyrosine Recognition by the Chemokine SDF-1/CXCL12
Veldkamp, C. T., Seibert, C., Peterson, F. C., De la Cruz, N. B., Haugner, J. C., Basnet, H., Sakmar, T. P., & Volkman, B. F. (2008) · Science Signaling · doi:10.1126/scisignal.1160755 · Cited by 287
Human cytomegalovirus encodes three G protein-coupled receptor homologues
Chee, M. S., Satchwell, S. C., Preddie, E. C., Weston, K., & Barrell, B. G. (1990) · Nature · doi:10.1038/344774a0 · Cited by 276
Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II
Deupi, X., Edwards, P., Singhal, A., Nickle, B., Oprian, D., Schertler, G., & Standfuss, J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1114089108 · Cited by 242
Brelot, A., Heveker, N., Montes, M., & Alizon, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000776200 · Cited by 236
Alpaca (Lama pacos) as a convenient source of recombinant camelid heavy chain antibodies (VHHs)
Maass, D. R., Sepulveda, J., Pernthaner, A., & Shoemaker, C. B. (2007) · Journal of Immunological Methods · doi:10.1016/j.jim.2007.04.008 · Cited by 214
Viral hijacking of G-protein-coupled-receptor signalling networks
Sodhi, A., Montaner, S., & Gutkind, J. S. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1529 · Cited by 174
GPCRDB: an information system for G protein-coupled receptors
Ísberg, V., Vroling, B., van der Kant, R., Li, K., Vriend, G., & Gloriam, D. E. I. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1255 · Cited by 153
Dukkipati, A., Park, H. H., Waghray, D., Fischer, S., & García, K. C. (2008) · Protein Expression and Purification · doi:10.1016/j.pep.2008.08.004 · Cited by 143
Self-citationMizoue, L. S., Bazán, J. F., Johnson, E. C., & Handel, T. M. (1999) · Biochemistry · doi:10.1021/bi9820614 · Cited by 142
Engineering Antibody Affinity by Yeast Surface Display
Colby, D. W., Kellogg, B. A., Graff, C. P., Yeung, Y. A., Swers, J. S., & Wittrup, K. D. (2004) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(04)88027-3 · Cited by 139
Burstein, E. S., Spalding, T. A., & Brann, M. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.38.24322 · Cited by 119
Waldhoer, M., Casarosa, P., ROSENKILDE, M. M., Smit, M. J., Leurs, R., Whistler, J. L., & Schwartz, T. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213179200 · Cited by 111
Herpesvirus-encoded GPCRs: neglected players in inflammatory and proliferative diseases?
Vischer, H. F., Siderius, M. H., Leurs, R., & Smit, M. J. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4189 · Cited by 91
Large-scale evaluation of protein reductive methylation for improving protein crystallization
Kim, Y., Quartey, P., Li, H., Volkart, L., Hatzos, C., Chang, C., Nocek, B. P., Cuff, M. E., Osipiuk, J., Tan, K., et al. (2008) · Nature Methods · doi:10.1038/nmeth1008-853 · Cited by 90
Gilliland, C. T., Salanga, C. L., Kawamura, T., Trejo, J., & Handel, T. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.503797 · Cited by 88
Function, diversity and therapeutic potential of the N-terminal domain of human chemokine receptors
Szpakowska, M., Fiévez, V., Arumugan, K., van Nuland, N. A. J., Schmit, J., & Chevigné, A. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.08.008 · Cited by 87
Vischer, H. F., Leurs, R., & Smit, M. J. (2005) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2005.11.006 · Cited by 79
Millard, C. J., Ludeman, J. P., Canals, M., Bridgford, J. L., Hinds, M. G., Clayton, D. J., Christopoulos, A., Payne, R. J., & Stone, M. J. (2014) · Structure · doi:10.1016/j.str.2014.08.023 · Cited by 75
The Crystal Structure of the Chemokine Domain of Fractalkine Shows a Novel Quaternary Arrangement
Hoover, D. M., Mizoue, L. S., Handel, T. M., & Lubkowski, J. T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002584200 · Cited by 59
Lipidic cubic phases as matrices for membrane protein crystallization
Nollert, P. (2004) · Methods · doi:10.1016/j.ymeth.2004.03.030 · Cited by 58
Xue, X., Lu, Q., Wei, H., Wang, D., Chen, D., He, G., Huang, L., Wang, H., & Wang, X. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002162 · Cited by 42
Constitutively Active Chemokine CXC Receptors
Han, X. (2014) · Advances in pharmacology · doi:10.1016/b978-0-12-417197-8.00009-2 · Cited by 31
Cited by
Molecular Dynamics Simulation for All
Hollingsworth, S. A., & Dror, R. O. (2018) · Neuron · doi:10.1016/j.neuron.2018.08.011 · Cited by 3,257
Self-citationThe Molecular Basis of G Protein–Coupled Receptor Activation
Weis, W. I., & Kobilka, B. K. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033910 · Cited by 1,227
GPCR Dynamics: Structures in Motion
Latorraca, N. R., Venkatakrishnan, A. J., & Dror, R. O. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00177 · Cited by 835
Self-citationStructure of CC chemokine receptor 2 with orthosteric and allosteric antagonists
Zheng, Y., Qin, L., Zacarías, N. V. O., de Vries, H., Han, G. W., Gustavsson, M., Dabros, M., Zhao, C., Cherney, R. J., Carter, P., et al. (2016) · Nature · doi:10.1038/nature20605 · Cited by 284
Core protein: A pleiotropic keystone in the HBV lifecycle
Zlotnick, A., Venkatakrishnan, B., Tan, Z., Lewellyn, E., Turner, W., & Francis, S. (2015) · Antiviral Research · doi:10.1016/j.antiviral.2015.06.020 · Cited by 268
Metadata
- Authors
- Burg, J. S., Ingram, J. R., Venkatakrishnan, A. J., Jude, K. M., Dukkipati, A., Feinberg, E. N., Angelini, A., Waghray, D., Dror, R. O., Ploegh, H. L., & Garcia, K. C.
- Venue
- Science
- Published
- 2015-03-06
- Volume
- 347
- Issue
- 6226
- Pages
- 1113-1117
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1988778953
- Cited by
- 273
- References
- 61
- FWCI
- 16.21
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
