The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid
Open accessAbstract
The HIV-1 capsid protein forms the conical core structure at the center of the mature virion. Capsid also binds the human peptidyl prolyl isomerase, cyclophilin A, thereby packaging the enzyme into the virion. Cyclophilin A subsequently performs an essential function in HIV-1 replication, possibly helping to disassemble the capsid core upon infection. We report the 2.36 A crystal structure of the N-terminal domain of HIV-1 capsid (residues 1-151) in complex with human cyclophilin A. A single exposed capsid loop (residues 85-93) binds in the enzyme's active site, and Pro-90 adopts an unprecedented trans conformation. The structure suggests how cyclophilin A can act as a sequence-specific binding protein and a nonspecific prolyl isomerase. In the crystal lattice, capsid molecules assemble into continuous planar strips. Side by side association of these strips may allow capsid to form the surface of the viral core. Cyclophilin A could then function by weakening the association between capsid strips, thereby promoting disassembly of the viral core.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“A beta-hairpin is formed by the N-terminal residues in mature-like CA, stabilized by a salt bridge between the N-terminal proline and a conserved aspartate in helix 3”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [72]
Citations
Cites
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581 · cited 1×
“Cyclophilin A is (bonds) 5 0.005 Å; RMSD (angles) 5 1.38; there are no w,c angles required for the replication of group M human immunodeficiency in the forbidden range (Laskowski et al., 1993).”
BackgroundInfluentialMOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011 · cited 1×
“(B) and (C) were prepared with MOLSCRIPT (Kraulis, 1991) and RASTER 3D (Bacon and Anderson, 1988). about CA151 residues 86 and 98, so that CypA and CA151 CypA active site groove.”
MethodJones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616 · cited 1×
“Mode of action of SDZ NIM spersed with model building using O (Jones et al., 1991).”
MethodLIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
Wallace, A. C., Laskowski, R. A., & Thornton, J. M. (1995) · Protein Engineering Design and Selection · doi:10.1093/protein/8.2.127 · Cited by 5,731 · cited 1×
“Schematic representation of the CA151 and CypA interface (Wallace et al., 1995).”
BackgroundAMoRe: an automated package for molecular replacement
Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,941
X-PLOR Version 3.1: A System for X-ray Crystallography and NMR
Brünger, A. T. (1992) · Medical Entomology and Zoology · Cited by 3,424
The mechanism of action of cyclosporin A and FK506
Schreiber, S. L., & Crabtree, G. R. (1992) · Immunology Today · doi:10.1016/0167-5699(92)90111-j · Cited by 2,127 · cited 1×
“Schreiber and Crabtree have proposed that CypA does not normally function as an enzyme in vivo However, it is possible that kcat/Km is similar to that of other substrates because kcat and Km have been(Schreiber and Crabtree, 1992).”
BackgroundImproved Fourier coefficients for maps using phases from partial structures with errors
Read, R. J. (1986) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767386099622 · Cited by 1,870
PROMOTIF—A program to identify and analyze structural motifs in proteins
Hutchinson, E. G., & Thornton, J. M. (1996) · Protein Science · doi:10.1002/pro.5560050204 · Cited by 1,043 · cited 1×
“The last six residues of both CA151 molecules are (A) Secondary structure of CA151 (Hutchinson and Thornton, 1996).”
BackgroundHuman Retroviruses and Aids - 1999
KUIKEN, C. L., & Foley, B. T. (1999) · doi:10.2172/1186019 · Cited by 952
Research works printed but not linked: 3
- Cowtan, 1994, ′dm′, Joint CCP, 34
- Gelderblom, H.R., Bauer, P.G.Özel, M., Höglund, S., Niedrig, M., Renz, H., Morath, B., Lundquist, P., NilssonÅ., Mattow, J., et al. (1992). Morphogenesis and morphology of human immunodeficiency virus. In Membrane Interactions of HIV, R.C. Aloia, and C.C. Curtain, eds. (New York: Wiley-Liss, Inc.), pp. 33–54.
- Otwinowski, Z. (1993). Oscillation data reduction program. In Data Collection and Processing, L. Sawyer, N. Isaacs, and S. Bailey, eds. (Warrington, England: SERC Daresbury Laboratory), pp. 56–62.
Cited by
Sorted by citations
Items 501–600 of 710
Urano, E., Kuramochi, N., Ichikawa, R., Murayama, S. Y., Miyauchi, K., Tomoda, H., Takebe, Y., Nermut, M. V., Komano, J. A., & Morikawa, Y. (2011) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00299-11 · Cited by 13
“225 and 226) (11, 16) were carried out by overlap PCR in the context of”
BackgroundMethodWang, F., Chen, J., Liu, X., Shen, X., He, X., Jiang, H., & Bai, D. (2006) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.54.372 · Cited by 13
Auerbach, M. R., Brown, K. R., Kaplan, A., Nueces, D. D. L., & Singh, I. R. (2006) · Journal of Virology · doi:10.1128/jvi.80.6.2884-2893.2006 · Cited by 13
“During assembly the CA domain is thought to mediate Gag-Gag interactions ( 16 , 18, 28, 35, 47).”
BackgroundEvolution of feline immunodeficiency virus Gag proteins
Burkala, E. J., & Poss, M. L. (2007) · Virus Genes · doi:10.1007/s11262-006-0058-8 · Cited by 13
In Vitro Processing of Human Immunodeficiency Virus Type 1 Gag Virus-like Particles
Morikawa, Y., Shibuya, M., Goto, T., & Sano, K. (2000) · Virology · doi:10.1006/viro.2000.0370 · Cited by 13
HIV protease substrate conformation: modulation by cyclophilin A
McCornack, M. A., Kakalis, L. T., Caserta, C., Handschumacher, R. E., & Armitage, I. M. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00974-5 · Cited by 13
Virus–Host Interactions in Retrovirus Integration
Engelman, A. N., & Maertens, G. N. (2018) · Retrovirus-Cell Interactions · doi:10.1016/b978-0-12-811185-7.00004-2 · Cited by 12
Samsudin, F., Gan, S. K.-E., & Bond, P. J. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2020.12.022 · Cited by 16
“region in the N-terminal domain of the latter [55].”
BackgroundInfluentialAntiviral Properties of HIV-1 Capsid Inhibitor GSK878
Wang, C., Huang, H., Mallon, K., Valera, L., Parcella, K. E., Cockett, M. I., Kadow, J. F., Gillis, E. P., Krystal, M., & Fridell, R. A. (2023) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01694-22 · Cited by 13
“74 (48), resides within the CA cyclophilin A (CypA) binding loop, distal to the inhibitor binding pocket (5, 46).”
BackgroundSagar, A., Herranz-Trillo, F., Langkilde, A. E., Vestergaard, B., & Bernadó, P. (2021) · Structure · doi:10.1016/j.str.2021.03.017 · Cited by 12
HIV-1 mutants that escape the cytotoxic T-lymphocytes are defective in viral DNA integration
Balasubramaniam, M., Davids, B.-O., Bryer, A., Xu, C., Thapa, S., Shi, J., Aiken, C., Pandhare, J., Perilla, J. R., & Dash, C. (2022) · PNAS Nexus · doi:10.1093/pnasnexus/pgac064 · Cited by 11
Sarkar, S., Balakrishnan, K., Chintala, K., Mohareer, K., Luedde, T., Vasudevan, A. A. J., Münk, C., & Banerjee, S. (2022) · Viruses · doi:10.3390/v14112503 · Cited by 13
“CYPA, a cytosolic peptidyl-prolyl isomerase, is known to bind to the proline-rich region, namely CYPA binding loop, in the N-terminal domain of HIV-1 CA [60].”
BackgroundHe, C., Gouble, A., Bourdel, A., Manchev, V. T., Poirot, L., Pâques, F., Duchateau, P. N., Edelman, A., & Danos, O. (2014) · Gene Therapy · doi:10.1038/gt.2014.51 · Cited by 11
Susceptibility and adaptation to human TRIM5α alleles at positive selected sites in HIV-1 capsid
Rahm, N., Gfeller, D., Snoeck, J., Martínez, R., McLaren, P. J., Ortiz, M., Ciuffi, A., & Telenti, A. (2013) · Virology · doi:10.1016/j.virol.2013.03.021 · Cited by 12
Intersubtype Differences in the Effect of a Rare p24 Gag Mutation on HIV-1 Replicative Fitness
Chopera, D., Cotton, L. A., Zawaira, A., Mann, J. K., Ngandu, N. K., Ntale, R. S., Carlson, J. M., Mlisana, K. P., Woodman, Z., Rosa, D. D. A., et al. (2012) · Journal of Virology · doi:10.1128/jvi.02171-12 · Cited by 12
“(A) N-terminal domain of p24 (PDB ID 1AK4 [23]) showing helix 6 (in color) and positions 248 (cyan) and 250 (red).”
Rong, L., Russell, R. S., Hu, J., Guan, Y., Kleiman, L., Liang, C., & Wainberg, M. A. (2001) · Journal of Virology · doi:10.1128/jvi.75.16.7230-7243.2001 · Cited by 12
“Secondary structural domains in the amino terminus of CA protein (amino acids 1 to 151) are illustrated that include a b-hairpin (b), seven a-helixes (H1 to H7), and a cyclophilin A (Cyp A) binding site located between H4 and H5 (14).”
BackgroundTandon, H., de Brevern, A. G., & Srinivasan, N. (2020) · Structure · doi:10.1016/j.str.2020.11.015 · Cited by 10
Ingram, Z., Fischer, D. K., & Ambrose, Z. (2021) · Viruses · doi:10.3390/v13112237 · Cited by 12
Targeting human immunodeficiency virus type 1 assembly, maturation and budding.
Wapling, J., Srivastava, S., Shehu-Xhilaga, M., & Tachedjian, G. (2007) · Europe PMC (PubMed Central) · Cited by 11
Fragile X mental retardation protein restricts replication of human immunodeficiency virus type 1
Pan, Q., Rong, L., Zhao, X., & Liang, C. (2009) · Virology · doi:10.1016/j.virol.2009.02.006 · Cited by 11
Hou, X., Liu, R. R., Huang, C., Jiang, L., Zhou, Y. J., & Chen, Q. (2017) · Cancer Biomarkers · doi:10.3233/cbm-170142 · Cited by 11
“Initial studies mainly focused on its role in protein folding, immune response and HIV-1 infection [21–23].”
Targeting the Early Step of Building Block Organization in Viral Capsid Assembly
Lampel, A., Bram, Y., Ezer, A., Shaltiel‐Karyo, R., Saad, J. S., Bacharach, E., & Gazit, E. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00347 · Cited by 11
Liang, W., Zhang, Y., Li, M., Al‐Shaebi, F., Li, J., Zhang, J., & Wei, L. (2021) · Journal of Virology · doi:10.1128/jvi.00563-21 · Cited by 11
A molecular dynamics study of Cyclophilin A free and in complex with the Ala-Pro dipeptide
Mark, P., & Nilsson, L. (2007) · European Biophysics Journal · doi:10.1007/s00249-006-0121-3 · Cited by 11
“1995); it has been reported to bind human immunodeficiency virus type 1 (HIV-1) gag protein (Gamble et al. 1996; Yoo et al. 1997; Zhao et al. 1997) to be required for the infectious activity of HIV-1 virions, where it is the first protein found to be incorporated into the virion during virus assembly and to perform an…”
BackgroundSharma, N., Ethiraj, K. R., Yadav, M., Nayarisseri, A., Chaurasiya, M., Vankudavath, R. N., & Rao, K. R. (2012) · Current Topics in Medicinal Chemistry · doi:10.2174/156802612803989309 · Cited by 12
National Synchrotron Light Source Activity Report 1998
Rothman, E. (1999) · doi:10.2172/770703 · Cited by 11
Martin, T., Lou, Y., Chou, C., Wei, S., Sadotra, S., Cho, C., Lin, M.-H., Tai, J.-H., Hsu, C., & Chen, C. (2018) · Scientific Reports · doi:10.1038/s41598-018-23821-5 · Cited by 10
The Magic of Linking Rings: Discovery of a Unique Photoinduced Fluorescent Protein Crosslink
Lu, M., Toptygin, D. D., Xiang, Y., Shi, Y., Schwieters, C. D., Lipinski, E. C., Ahn, J., Byeon, I. L., & Gronenborn, A. M. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c02054 · Cited by 10
Hou, J., Zhang, Q., Liu, Z., Wang, S., Li, D., Liu, C., Liu, Y., & Shao, Y. (2015) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2015.1082692 · Cited by 10
“Moreover, the interactions between CyPA and the Gag protein have been investigated for decades.(9-11) Previous studies demonstrated that CyPA was a specific host factor that was incorporated into HIV-1 virions but not into other primate immunodeficiency viruses (SIV and HIV-2).”
BackgroundProductive Replication and Evolution of HIV-1 in Ferret Cells
Fadel, H. J., Saenz, D. T., Guevara, R. B., von Messling, V., Peretz, M., & Poeschla, E. M. (2011) · Journal of Virology · doi:10.1128/jvi.06035-11 · Cited by 10
“8E); sequencing and determination of the 345 predicted amino acid seqence did not reveal significant differences in the known HIV-1 346 capsid interacting regions (14, 21, 72).”
BackgroundMonte Carlo Simulations of HIV Capsid Protein Homodimer
Zhu, F., & Chen, B. (2015) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5b00126 · Cited by 11
“1), we treat the NTD (1-145) and the CTD (151-219) as two rigid domains, and the linker (146-150) as a flexible chain.”
Lanman, J. K., & Prevelige, P. E. (2005) · Advances in virus research · doi:10.1016/s0065-3527(05)64009-2 · Cited by 10
Lai, D., SINGH, S. P., Cartas, M. A., Murali, R., Kalyanaraman, V. S., & Srinivasan, A. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01264-3 · Cited by 10
Isolation and characterization of a small antiretroviral molecule affecting HIV-1 capsid morphology
Abdurahman, S., Végvári, Á., Levi, M., Höglund, S., Högberg, M., Tong, W., Romero, I., Balzarini, J. M., & Vahlne, A. G. (2009) · Retrovirology · doi:10.1186/1742-4690-6-34 · Cited by 10
“The conical core formation not only results as a consequence of the proteolytic cleavage of p55 but also from substantial conformational changes and rearrangements of the p24 [1] which is connected to one another through N-terminal hexamer and C-terminal dimer formations [5-8].”
BackgroundBarrera, F. N., Hurtado-Gómez, E., Lidón‐Moya, M. C., & Neira, J. L. (2006) · Biochemical Journal · doi:10.1042/bj20051487 · Cited by 10
Cyclophilin A facilitates HIV-1 integration
Padron, A., Dwivedi, R., Chakraborty, R., Prakash, P., Kim, K., Shi, J., Ahn, J., Pandhare, J., Luban, J., Aiken, C., et al. (2024) · Journal of Virology · doi:10.1128/jvi.00947-24 · Cited by 10
“Specifically, CypA was demonstrated to bind to the proline-rich CypA-binding loop of the HIV-1 CA-NTD region (65–67).”
InfluentialCurvature of the Retroviral Capsid Assembly Is Modulated by a Molecular Switch
Thames, T., Bryer, A. J., Qiao, X., Jeon, J., Weed, R., Janicki, K., Hu, B., Gor’kov, P. L., Hung, I., Gan, Z., et al. (2021) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.1c01769 · Cited by 9
Targeting Human Immunodeficiency Virus Type 1 Assembly, Maturation and Budding
Wapling, J., Srivastava, S., Shehu-Xhilaga, M., & Tachedjian, G. (2007) · Drug Target Insights · doi:10.1177/117739280700200020 · Cited by 11
“The C-terminal domain of CA (C-CA) or the CTD, is critical for Gag-Gag interactions during assembly and maturation (Gamble et al. 1996; Gamble et al. 1997) and described mutations in this region have major consequences on virion maturation and infectivity (von Schwedler et al. 2003;…”
Human immunodeficiency virus-1 core: The Trojan horse in virus–host interaction
Wang, W., Li, Y., Zhang, Z., & Wei, W. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.1002476 · Cited by 9
“, 2021), N-terminal domain of CA (NTDs) which contains seven α helices and a cyclophilin A (CypA)-binding loop forms hexamers through an NTD-NTD interface (Gamble et al., 1996), C-terminal domain of CA (CTDs) forms dimers with adjacent hexamers through a CTD–CTD interface (Gamble et al.”
BackgroundLampel, A., Yaniv, O., Berger, O., Bacharach, E., Gazit, E., & Frolow, F. (2013) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309113011871 · Cited by 9
“…have determined several high-resolution structures of isolated CA domains and of fulllength CA (Gitti et al., 1996; Berthet-Colominas et al., 1999; Gamble et al., 1996, 1997; Kelly et al., 2006; Momany et al., 1996; Ternois et al., 2005; Worthylake et al., 1999; Tang et al., 2002; Wong et al.,…”
BackgroundImproving HIV proteome annotation: new features of BioAfrica HIV Proteomics Resource
Druce, M., Hulo, C., Masson, P., Sommer, P., Xénarios, I., Mercier, P. L., & de Oliveira, T. (2016) · Database · doi:10.1093/database/baw045 · Cited by 9
Paediatric non-progression following grandmother-to-child HIV transmission
Tsai, M.-H., Muenchhoff, M., Adland, E., Carlqvist, A., Roider, J., Cole, D. K., Sewell, A. K., Carlson, J. M., Ndung’u, T., & Goulder, P. (2016) · Retrovirology · doi:10.1186/s12977-016-0300-y · Cited by 9
Neira, J. L. (2009) · The Scientific World JOURNAL · doi:10.1100/tsw.2009.52 · Cited by 8
“helices, with two additional short α-helices following an extended proline-rich loop[16,17,18].”
BackgroundInfluentialCrystals of Rous Sarcoma Virus Capsid Protein Show a Helical Arrangement of Protein Subunits
Kovari, L. C., Momany, C., Miyagi, F., Lee, S., Campbell, S., Vuong, B. Q., Vogt, V. M., & Rossmann, M. G. (1997) · Virology · doi:10.1006/viro.1997.8807 · Cited by 9
“Biol.CA (Gamble et al., 1996; Momany et al., 1996).”
BackgroundInfluentialIFI27 inhibits HIV-1 replication by degrading Gag protein through the ubiquitin-proteasome pathway
He, W.-Q., Pang, W. K., Li, N., Li, A.-Q., Li, Y., Lu, Y., Shen, F., Xin, R., Song, T., Tian, R., et al. (2024) · Journal of Virology · doi:10.1128/jvi.01356-24 · Cited by 8
A new functional role of HIV-1 integrase during uncoating of the viral core
Briones, M., & Chow, S. A. (2010) · Immunologic research · doi:10.1007/s12026-010-8164-z · Cited by 12
Brun, S., Chaloin, L., Gay, B., Bernard, É., Devaux, C. A., Lionne, C., Chazal, N., & Briant, L. (2010) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22729 · Cited by 8
Kamada, K., Yoshida, A., Khamsri, B., Piroozmand, A., Yamashita, T., Uchiyama, T., Fujita, M., & Adachi, A. (2006) · Microbes and Infection · doi:10.1016/j.micinf.2005.11.006 · Cited by 8
Role of Cyclophilin A in HIV Replication
Votteler, J., Wray, V., & Schubert, U. (2006) · Future Virology · doi:10.2217/17460794.2.1.65 · Cited by 8
“Gag and CsA were later found to compete for the same binding site in CypA, although the CypA–Gag complex does not interfere with calcineurin [51,53,54].”
BackgroundInfluentialThe Early Bird Catches the Worm - Can Evolution Teach us Lessons in Fighting HIV?
Schaller, T., & Herold, N. (2016) · Current HIV Research · doi:10.2174/1570162x14999160224094914 · Cited by 8
Molecular characteristics and prevalence of small ruminant lentiviruses in goats in Japan
Kokawa, S., Oba, M., Hirata, T., Tamaki, S., Omura, M., Tsuchiaka, S., Nagai, M., Omatsu, T., & Mizutani, T. (2017) · Archives of Virology · doi:10.1007/s00705-017-3447-5 · Cited by 8
“The importance of the MHR is that it accounts for the diversity of phenotypes and its immune response [40].”
BackgroundSong, B. (2009) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-02175-6_3 · Cited by 8
Network analysis of protein-protein interaction
Chang, S., Gong, X., Jiao, X., Li, C., Chen, W., & Wang, C. (2010) · Chinese Science Bulletin · doi:10.1007/s11434-009-0742-x · Cited by 8
Nakayama, E. E., Shingai, Y., Kono, K., & Shioda, T. (2008) · Virology · doi:10.1016/j.virol.2008.02.028 · Cited by 8
Specific nature of cellular immune responses elicited by chimpanzees against HIV-1
Balla-Jhagjhoorsingh, S. S., Verschoor, E. J., de Groot, N., Teeuwsen, V. J. P., Bontrop, R. E., & Heeney, J. L. (2003) · Human Immunology · doi:10.1016/s0198-8859(03)00088-0 · Cited by 8
“Both epitopes were located in the same Gag-p24/CA region involved in essential functions in HIV replication [46].”
BackgroundDick, A., Meuser, M. E., & Cocklin, S. (2022) · Biomolecules · doi:10.3390/biom12050695 · Cited by 7
Taylor, I. A., & Fassati, A. (2023) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjad076 · Cited by 7
“CypA binds to the capsid at the so-called Cyp-loop, which is positioned between helices α 4 and α 5 on the outer surface of the CA-NTD ( Figure 1 A; Gamble et al., 1996 ) .”
BackgroundComputational Validation of Protein Nanotubes
Buch, I., Brooks, B. R., Wolfson, H. J., & Nussinov, R. (2009) · Nano Letters · doi:10.1021/nl803521j · Cited by 7
Zhang, P., Meng, X., & Zhao, G. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-176-9_21 · Cited by 7
Properties that rank protein:protein docking poses with high accuracy
Simões, I. C. M., Coimbra, J. T. S., Neves, R. P. P., Costa, I. P. D., Ramos, M. J., & Fernandes, P. A. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c8cp03888k · Cited by 7
Hybrid Vigor: Hybrid Methods In Viral Structure Determination
Gilbert, R. J. C., Grimes, J. M., & Stuart, D. I. (2003) · Advances in protein chemistry · doi:10.1016/s0065-3233(03)01002-7 · Cited by 7
Khan, M. B., Garcia-Barrio, M. T., & Powell, M. D. (2003) · Journal of Virology · doi:10.1128/jvi.77.7.4431-4434.2003 · Cited by 7
“Specifically, CyPA can bind to CA (14) and modify the folding of CA to potentially influence the structure of the mature core (1, 5).”
BackgroundCyclophilin A Regulates Tripartite Motif 5 Alpha Restriction of HIV-1
Wang, T., Becker, D., Twizerimana, A. P., Luedde, T., Gohlke, H., & Münk, C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26020495 · Cited by 6
“The CA-NTD consists of seven α -helices and a characteristic extended CYPA-binding loop [55] (Figure 3C).”
Help or Hinder: Protein Host Factors That Impact HIV-1 Replication
Moezpoor, M. R., & Stevenson, M. (2024) · Viruses · doi:10.3390/v16081281 · Cited by 7
Cell Type-Dependent Escape of Capsid Inhibitors by Simian Immunodeficiency Virus SIVcpz
Twizerimana, A. P., Scheck, R., Becker, D., Zhang, Z., Wammers, M., Avelar, L. A. A., Pflieger, M., Häussinger, D., Kurz, T., Gohlke, H., et al. (2020) · Journal of Virology · doi:10.1128/jvi.01338-20 · Cited by 6
Chiu, H.-C., Wang, F., Yao, S., & Wang, C.-T. (2002) · Journal of Medical Virology · doi:10.1002/jmv.10197 · Cited by 6
“Cyclophilin A appears to be incorporated into virions via interaction with Gag precursor Pr55gag, and gag sequences responsible for cyclophilin A incorporation have been mapped to the N-terminal capsid region [Franke et al., 1994; Thali et al., 1994; Colgan et al., 1996; Gamble et al., 1996].”
The pH dependence of HIV-1 capsid assembly and its interaction with cyclophilin A.
Bonhomme, M., Wong, S., Carter, C., & Scarlata, S. (2003) · Biophysical Chemistry · doi:10.1016/s0301-4622(03)00063-2 · Cited by 8
Hantson, A., Fikkert, V., Remoortel, B. V., Pannecouque, C. C., Cherepanov, P., Matthews, B. R., Holan, G., Clercq, E. D., Vandamme, A., Debyser, Z., et al. (2005) · Antiviral chemistry & chemotherapy · doi:10.1177/095632020501600405 · Cited by 6
“It has been suggested that CyPA promotes disassembly of the viral core during uncoating by weakening the association of the CA proteins (Gamble et al., 1996).”
BackgroundKurts, C., Carbone, F., Krummel, M. F., Koch, K. M., MILLER, J. F. A. P., & Heath, W. R. (2000) · Nature · doi:10.1038/35030185 · Cited by 6
Cyclophilins: The Structure and Functions of an Important Peptidyl-prolyl Isomerase
Idris, M. O., Idris, M., Fadahunsi, A. A., & Sedzro, D. M. (2019) · International Journal of Biochemistry Biophysics & Molecular Biology · doi:10.11648/j.ijbbmb.20190401.11 · Cited by 5
A computational framework for modeling functional protein‐protein interactions
Pal, A., Pal, D., & Mitra, P. (2021) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26156 · Cited by 5
CP-MAS and Solution NMR Studies of Allosteric Communication in CA-assemblies of HIV-1
Nicastro, G., Lucci, M., Oregioni, A., Kelly, G. P., Frenkiel, T. A., & Taylor, I. A. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167691 · Cited by 5
Shah, V. B., & Aiken, C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092724 · Cited by 6
Lipid directed assembly of the HIV capsid protein
Miles, P., & Frankel, D. J. (2014) · Soft Matter · doi:10.1039/c4sm01860e · Cited by 5
Potential Role for CA-SP in Nucleating Retroviral Capsid Maturation
England, M. R., Purdy, J. G., Ropson, I. J., Dalessio, P. M., & Craven, R. C. (2014) · Journal of Virology · doi:10.1128/jvi.00309-14 · Cited by 5
Twizerimana, A. P., Becker, D., Zhu, S., Luedde, T., Gohlke, H., & Münk, C. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2306374120 · Cited by 4
“To confirm the expression of primate TRIM5 proteins, cells were lysed using RIPA lysis buffer [25 mM Tris - HCl (pH 8.0), 137 mM NaCl, 1% NP - 40, 1% glycerol, 0.5% sodium deoxycholate, 0.1% sodium dodecyl sulfate (SDS), 2 mM ethylenediaminetetraacetic acid (EDTA), and protease inhibitor cocktail…”
MethodInfluentialSIV replication in human cells
Sakuma, R., & Takeuchi, H. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00162 · Cited by 5
“The sequence Ala88-Gly89-Pro90-Ile91 of CA protein is the major fragment bound to the active site of CypA (Franke et al., 1994; Gamble et al., 1996; Zhao et al., 1997).”
BackgroundDesign and synthesis of peptide-based macrocyclic cyclophilin inhibitors
Granger, B. A., & Brown, D. G. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.09.039 · Cited by 5
Inhibitor-Based Therapeutics for Treatment of Viral Hepatitis
Dey, D., & Banerjee, M. (2016) · Journal of Clinical and Translational Hepatology · doi:10.14218/jcth.2016.00025 · Cited by 5
“CyPA was found to interact with the non-structural protein NS5A(69,70) of HCV and the capsid protein p24 of HIV.(71) Presently, two drugs that inhibit CyPA, namely alisporivir and SCY-635, are in use.”
BackgroundInfluentialExtracellular cyclophilin A as a humoral factor modulating cardiovascular inflammatory responses
Hattori, F. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.04.006 · Cited by 5
HIV-1 Gag shares a signature motif with annexin (Anx7), which is required for virus replication
Srivastava, M., Cartas, M. A., Rizvi, T. A., SINGH, S. P., Serio, D., Kalyanaraman, V. S., Pollard, H. B., & Srinivasan, A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.2704 · Cited by 5
Takemura, T., Kawamata, M., Urabe, M., & Murakami, T. (2013) · Journal of Virology · doi:10.1128/jvi.01319-12 · Cited by 4
Doménech, R., Bocanegra, R., Velázquez‐Campoy, A., & Neira, J. L. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.06.011 · Cited by 4
MOLECULAR CHARACTERIZATION OF PARTIAL SEQUENCES OF BRAZILIAN BLV GAG SEQUENCES
Camargos, M. F., dos Reis, J. K. P., & Leite, R. C. (2007) · VIRUS Reviews & Research · doi:10.17525/vrr.v12i1-2.9 · Cited by 4
“The p24 protein also contributes to gag polyprotein packing during viral assembly and it is important in the early stages of infection by interaction with cyclofilin A (Gamble et al. 1996).”
BackgroundZhang, W., Mendonça, L., & Mansky, L. M. (2018) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-10-8456-0_8 · Cited by 4
Hamilton, G. S., & Thomas, C. (2000) · Advances in medicinal chemistry · doi:10.1016/s1067-5698(00)80003-6 · Cited by 4
Virus crystallography and structural virology: a personal perspective
Rossmann, M. G. (2014) · Crystallography Reviews · doi:10.1080/0889311x.2014.957282 · Cited by 4
Xu, L., Yan, X., Luo, M., Guan, Y., & Yao, S. (2008) · Biotechnology Progress · doi:10.1021/bp070259m · Cited by 4
Lang, D. M. (2007) · Virology Journal · doi:10.1186/1743-422x-4-113 · Cited by 4
“E260 which is a region of small helices and loops adjacent to the CypA binding site that is probably essential to disassembling the core upon infection [14]; these mIMRs, then, begin at sequences that localize Gag to the cell membrane – a process essential to core formation – and end at sequences that dissolve the vir…”
BackgroundInfluentialNagao, T., Hatcho, K., Doi, N., Fujiwara, S., Adachi, A., & Nomaguchi, M. (2009) · The Journal of Medical Investigation · doi:10.2152/jmi.56.21 · Cited by 4
Doménech, R., Bocanegra, R., González‐Muñiz, R., Gómez, J., Mateu, M. G., & Neira, J. L. (2011) · Biomacromolecules · doi:10.1021/bm2007168 · Cited by 4
Optimization of Cyclophilin Inhibitors for Use in Antiviral Therapy
Peel, M. R., & Scribner, A. W. (2013) · Royal Society of Chemistry eBooks · doi:10.1039/9781849737814-00384 · Cited by 4
Structural Biology of HIV Assembly
de Marco, A., Kräusslich, H., & Briggs, J. A. G. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7729-7_1 · Cited by 4
“The structures of both domains have been solved at atomic resolution [ 18 – 20 ].”
BackgroundJuárez‐Jiménez, J., Tew, P., O’Connor, M. B., Llabrés, S., Sage, R., Glowacki, D. R., & Michel, J. (2020) · ChemRxiv · doi:10.26434/chemrxiv.11833470.v2 · Cited by 4
Systematic discovery of pro- and anti-HIV host factors in primary human CD4+ T cells
Rathore, U., Dugan, E. J., Thornton, H., Kumar, V. E., Dajani, R., Burdick, R. C., Young, J. M., Steinhart, Z., Lao, R., Delviks‐Frankenberry, K. A., et al. (2026) · Cell · doi:10.1016/j.cell.2026.03.046 · Cited by 4
Exploring the Structural Divergence of HIV and SRLV Lentiviral Capsids
Arizaga, F., Freniere, C., Rey, J. S., Cook, M., Wu, C., Perilla, J. R., & Xiong, Y. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c09436 · Cited by 5
Keeping your armour intact: How HIV‐1 evades detection by the innate immune system
Maelfait, J., Seiradake, E., & Rehwinkel, J. (2014) · BioEssays · doi:10.1002/bies.201400019 · Cited by 3
Pao, P.-J., Hsu, M., Chiang, M.-H., Chen, C., Lee, C., & Wang, A. H. ‐. (2021) · FEBS Journal · doi:10.1111/febs.16184 · Cited by 3
Role of peptidyl-prolyl cis–trans isomerases in infectious diseases and host–pathogen interactions
Biswas, G., & Banerjee, R. (2021) · Current Science · doi:10.18520/cs/v121/i6/758-768 · Cited by 3
Structural adaptability of SARS-CoV-2 Nsp1 with the host network
Padariya, M., Hupp, T. R., & Kalathiya, U. (2025) · European Biophysics Journal · doi:10.1007/s00249-025-01762-y · Cited by 3
“Though the binding of Nsp1 and immuno-philins (Pfefferle et al. 2011; Gamble et al. 1996; Davis et al. 2010; Reidt et al. 2003; Schultz and Clardy 1998; Deiva-nayagam et al. 2000) is known, the molecular level details of these protein networks remain elusive, and therefore, applying structural…”
Metadata
- Authors
- Gamble, T. R., Vajdos, F. F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I., & Hill, C. P.
- Affiliations
- University of Utah (US)
- Corresponding author
- Hill, Christopher P
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1996-12
- Volume
- 87
- Issue
- 7
- Pages
- 1285-1294
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2121753315
- Cited by
- 706
- References
- 59
- Citations by year
- 2026: 12 · 2025: 8 · 2024: 7 · 2023: 18 · 2022: 20 · 2021: 26 · 2020: 16 · 2019: 12 · 2018: 23 · 2017: 21 · 2016: 29 · 2015: 22 · 2014: 25 · 2013: 32 · 2012: 24
- FWCI
- 6.27
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Keywords
- cyclophilin A, HIV-1 capsid, peptidyl-prolyl isomerase, protein-protein complex, capsid disassembly, viral core, capsid assembly, HIV-1 replication
- MeSH terms
- Amino Acid Isomerases, Capsid, Carrier Proteins, Humans, Models, Molecular, Protein Binding, Virion, HIV-1, Gene Products, gag, Protein Structure, Tertiary, Crystallography, X-Ray, Peptidylprolyl Isomerase
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
