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Journal articles on the topic 'Protein X'

Author: Grafiati

Published: 3 June 2025

Last updated: 31 July 2025

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1

Figarella, Catherine, Michèle Amouric, and Odette Guy-Crotte. "PANCREATIC STONE PROTEIN, PROTEIN X, AND THREAD PROTEIN." Lancet 329, no. 8526 (1987): 222–23. http://dx.doi.org/10.1016/s0140-6736(87)90042-0.

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2

Bennett, Pauline, Roger Starr, Arthur Elliott, and Gerald Offer. "The structure of C-protein and X-protein molecules and a polymer of X-protein." Journal of Molecular Biology 184, no. 2 (1985): 297–309. http://dx.doi.org/10.1016/0022-2836(85)90381-x.

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3

Lee, Sang-Hyeon, Hayao Taguchi, Etsuro Yoshimura, et al. "The active site of carboxypeptidase Taq possesses the active-site motif His–Glu–X–X-His of zinc-dependent endopeptidases and aminopeptidases." "Protein Engineering, Design and Selection" 9, no. 6 (1996): 467–69. http://dx.doi.org/10.1093/protein/9.6.467.

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4

Maggs, J. L., N. R. Kitteringham, P. S. Grabowski, and B. K. Park. "Drug-protein conjugates—X." Biochemical Pharmacology 35, no. 3 (1986): 505–13. http://dx.doi.org/10.1016/0006-2952(86)90227-3.

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5

Lau, S. Y., J. W. Siau, R. M. Sobota, et al. "Synthetic 10FN3-based mono- and bivalent inhibitors of MDM2/X function." Protein Engineering, Design and Selection 31, no. 7-8 (2018): 301–12. http://dx.doi.org/10.1093/protein/gzy018.

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6

Brown, R. M., R. A. Head, A. A. M, et al. "Pyruvate dehydrogenase E3 binding protein (protein X) deficiency." Developmental Medicine & Child Neurology 48, no. 9 (2007): 756–60. http://dx.doi.org/10.1111/j.1469-8749.2006.tb01362.x.

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7

Brown, RM, RA Head, AAM Morris, et al. "Pyruvate dehydrogenase E3 binding protein (protein X) deficiency." Developmental Medicine & Child Neurology 48, no. 09 (2006): 756. http://dx.doi.org/10.1017/s0012162206001617.

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8

Rypniewski, W. R., S. Hastrup, Ch Betzel, et al. "The sequence and X-ray structure of the trypsin from Fusarium oxysporum." "Protein Engineering, Design and Selection" 6, no. 4 (1993): 341–48. http://dx.doi.org/10.1093/protein/6.4.341.

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9

Assouline, Z., H. Shen, D. G. Kilburn, and R. A. J. Warren. "Production and properties of a factor X–cellulose-binding domain fusion protein." "Protein Engineering, Design and Selection" 6, no. 7 (1993): 787–92. http://dx.doi.org/10.1093/protein/6.7.787.

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10

Zheng, Wenjun, and Sebastian Doniach. "Fold recognition aided by constraints from small angle X-ray scattering data." Protein Engineering, Design and Selection 18, no. 5 (2005): 209–19. http://dx.doi.org/10.1093/protein/gzi026.

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11

Choonnasard, Amonrat, Maya Shofa, Tamaki Okabayashi, and Akatsuki Saito. "Conserved Functions of Orthohepadnavirus X Proteins to Inhibit Type-I Interferon Signaling." International Journal of Molecular Sciences 25, no. 7 (2024): 3753. http://dx.doi.org/10.3390/ijms25073753.

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Orthohepadnavirus causes chronic hepatitis in a broad range of mammals, including primates, cats, woodchucks, and bats. Hepatitis B virus (HBV) X protein inhibits type-I interferon (IFN) signaling, thereby promoting HBV escape from the human innate immune system and establishing persistent infection. However, whether X proteins of Orthohepadnavirus viruses in other species display a similar inhibitory activity remains unknown. Here, we investigated the anti-IFN activity of 17 Orthohepadnavirus X proteins derived from various hosts. We observed conserved activity of Orthohepadnavirus X proteins

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12

Jin, Bo, Jiayue Wang, Xiangnan Liu, et al. "Ubiquitin-Mimicking Peptides Transfer Differentiates by E1 and E2 Enzymes." BioMed Research International 2018 (August 30, 2018): 1–8. http://dx.doi.org/10.1155/2018/6062520.

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Ubiquitin and ubiquitin like proteins (UBLs) play key roles in eukaryotes. These proteins are attached to their target proteins through an E1-E2-E3 cascade and modify the functions of these proteins. Since the discovery of ubiquitin, several UBLs have been identified, including Nedd8, SUMO, ISG15, and Atg8. Ubiquitin and UBLs share a similar three-dimensional structure: β-grasp fold and an X-X-[R/A/E/K]-X-X-[G/X]-G motif at the C-terminus. We have previously reported that ubiquitin, Nedd8, and SUMO mimicking peptides which all contain the conserved motif X-X-[R/A/E/K]-X-X-[G/X]-G still retaine

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13

Lo, K. M., Y. Sudo, J. Chen, et al. "High level expression and secretion of Fc-X fusion proteins in mammalian cells." Protein Engineering Design and Selection 11, no. 6 (1998): 495–500. http://dx.doi.org/10.1093/protein/11.6.495.

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14

Facchiano, A. M., G. Colonna, and R. Ragone. "Helix stabilizing factors and stabilization of thermophilic proteins: an X-ray based study." Protein Engineering Design and Selection 11, no. 9 (1998): 753–60. http://dx.doi.org/10.1093/protein/11.9.753.

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15

Bergametti, Françoise, Delphine Sitterlin, and Catherine Transy. "Turnover of Hepatitis B Virus X Protein Is Regulated by Damaged DNA-Binding Complex." Journal of Virology 76, no. 13 (2002): 6495–501. http://dx.doi.org/10.1128/jvi.76.13.6495-6501.2002.

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ABSTRACT Mammalian hepatitis B viruses encode an essential regulatory protein, termed X, which may also be implicated in liver cancer development associated with chronic infection. X protein, also referred to as HBx in human virus and WHx in woodchuck virus, has been reported to bind to a number of cellular proteins, including the DDB1 subunit of the damaged DNA-binding (DDB) complex. Our previous work provided genetic evidence for the importance of WHx-DDB1 interaction in both the activity of the X protein and establishment of viral infection in woodchucks. In the present study, a direct acti

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16

Wadahama, Hiroyuki, Shinya Kamauchi, Masao Ishimoto, Teruo Kawada, and Reiko Urade. "Protein disulfide isomerase family proteins involved in soybean protein biogenesis." FEBS Journal 274, no. 3 (2006): 687–703. http://dx.doi.org/10.1111/j.1742-4658.2006.05613.x.

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17

Nchongboh, Chofong Gilbert, Guan-wei Wu, Ni Hong, and Guo-ping Wang. "Protein–protein interactions between proteins of Citrus tristeza virus isolates." Virus Genes 49, no. 3 (2014): 456–65. http://dx.doi.org/10.1007/s11262-014-1100-x.

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18

Krieg, Joachim, Steffen Hartmann, Anna Vicentini, Wolfgang Gläsner, Daniel Hess, and Jan Hofsteenge. "Recognition Signal for C-Mannosylation of Trp-7 in RNase 2 Consists of Sequence Trp-x-x-Trp." Molecular Biology of the Cell 9, no. 2 (1998): 301–9. http://dx.doi.org/10.1091/mbc.9.2.301.

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C2-α-Mannosyltryptophan was discovered in human RNase 2, an enzyme that occurs in eosinophils and is involved in host defense. It represents a novel way of attaching carbohydrate to a protein in addition to the well-known N- andO-glycosylations. The reaction is specific, as in RNase 2 Trp-7, but never Trp-10, which is modified. In this article, we address which structural features provide the specificity of the reaction. Expression of chimeras of RNase 2 and nonglycosylated RNase 4 and deletion mutants in HEK293 cells identified residues 1–13 to be sufficient for C-mannosylation. Site-directed

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19

Slifman, N. R., P. Venge, C. G. Peterson, D. J. McKean, and G. J. Gleich. "Human eosinophil-derived neurotoxin and eosinophil protein X are likely the same protein." Journal of Immunology 143, no. 7 (1989): 2317–22. http://dx.doi.org/10.4049/jimmunol.143.7.2317.

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Abstract The human eosinophil granule contains a series of cationic proteins. Two of these, eosinophil-derived neurotoxin (EDN) and eosinophil protein X (EPX), are reported to have similar m.w. and both possess neurotoxic and helminthotoxic activities. Therefore, the properties of these molecules were analyzed to determine whether they differ. EDN was purified from eosinophils of patients with the hypereosinophilic syndrome and EPX from the buffy coat cells of normal individuals. By SDS-PAGE, both proteins showed a major band at 18.7 kDa and a minor band at 21.4 kDa. By two-dimensional non-equ

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20

Chapman, Henry N., and John C. H. Spence. "Femtosecond X-ray protein nanocrystallography." Acta Crystallographica Section A Foundations of Crystallography 66, a1 (2010): s9. http://dx.doi.org/10.1107/s0108767310099836.

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21

Chapman, Henry N., Petra Fromme, Anton Barty, et al. "Femtosecond X-ray protein nanocrystallography." Nature 470, no. 7332 (2011): 73–77. http://dx.doi.org/10.1038/nature09750.

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22

Bonn, Dorothy. "Protein X and liver cancer." Lancet 341, no. 8845 (1993): 625. http://dx.doi.org/10.1016/0140-6736(93)90379-u.

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23

Feliciano, Pamela. "Fragile X protein stalls ribosomes." Nature Genetics 43, no. 9 (2011): 824. http://dx.doi.org/10.1038/ng.927.

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24

Mahdi, Mohamed, Tamás Richárd Linkner, Zsófia Ilona Szojka, and József Tőzsér. "Elucidating the Role of HIV-2 Viral Protein X." Proceedings 50, no. 1 (2020): 24. http://dx.doi.org/10.3390/proceedings2020050024.

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Human immunodeficiency viruses type 1 and 2 (HIV-1 and HIV-2) are the causative agents of the acquired immunodeficiency syndrome (AIDS). While both viruses share a similar structural and genomic organization, a difference in replication dynamics and the clinical course of infection is evident between the two. Patients dually infected were shown to have lower viral loads and generally a slower rate of progression to AIDS than those who are mono-infected. While the roles of the unique accessory proteins have been studied in detail for HIV-1, those of HIV-2, including viral protein X (Vpx), remai

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25

Klein, Claudio, Wolfgang Vogel, Hans Bender, and Georg E. Schulz. "Engineering a heavy atom derivative for the X-ray structure analysis of cyclodextrin glycosyltransferase." "Protein Engineering, Design and Selection" 4, no. 1 (1990): 65–67. http://dx.doi.org/10.1093/protein/4.1.65.

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26

Weston, Simon, and Dietrich Suck. "X-ray structures of two single-residue mutants of DNase I: H134Q and Y76A." "Protein Engineering, Design and Selection" 6, no. 4 (1993): 349–57. http://dx.doi.org/10.1093/protein/6.4.349.

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27

Scouras, A. D., and V. Daggett. "Disruption of the X-loop turn of the prion protein linked to scrapie resistance." Protein Engineering Design and Selection 25, no. 5 (2012): 243–49. http://dx.doi.org/10.1093/protein/gzs009.

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28

Clore, G. Marius, Angela M. Gronenborn, Michael N. G. James, Mogens Kjaer, Catherine A. McPhalen, and Fleming M. Poulsen. "Comparison of the solution and X-ray structures of barley serine proteinase inhibitor 2." "Protein Engineering, Design and Selection" 1, no. 4 (1987): 313–18. http://dx.doi.org/10.1093/protein/1.4.313.

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29

Williams, M. G., J. Wilsher, P. Nugent, et al. "Mutagenesis, biochemical characterization and X-ray structural analysis of point mutants of bovine chymosin." Protein Engineering Design and Selection 10, no. 9 (1997): 991–97. http://dx.doi.org/10.1093/protein/10.9.991.

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30

Tovchigrechko, A., and I. A. Vakser. "GRAMM-X public web server for protein-protein docking." Nucleic Acids Research 34, Web Server (2006): W310—W314. http://dx.doi.org/10.1093/nar/gkl206.

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31

Barak, Orr, Ami Aronheim, and Yosef Shaul. "HBV X Protein Targets HIV Tat-Binding Protein 1." Virology 283, no. 1 (2001): 110–20. http://dx.doi.org/10.1006/viro.2001.0883.

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32

Dobransky, Ashley, Mary Root, Nicholas Hafner, Matty Marcum, and H. John Sharifi. "CRL4-DCAF1 Ubiquitin Ligase Dependent Functions of HIV Viral Protein R and Viral Protein X." Viruses 16, no. 8 (2024): 1313. http://dx.doi.org/10.3390/v16081313.

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The Human Immunodeficiency Virus (HIV) encodes several proteins that contort the host cell environment to promote viral replication and spread. This is often accomplished through the hijacking of cellular ubiquitin ligases. These reprogrammed complexes initiate or enhance the ubiquitination of cellular proteins that may otherwise act to restrain viral replication. Ubiquitination of target proteins may alter protein function or initiate proteasome-dependent destruction. HIV Viral Protein R (Vpr) and the related HIV-2 Viral Protein X (Vpx), engage the CRL4-DCAF1 ubiquitin ligase complex to targe

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33

Allen, James P. "Recent innovations in membrane-protein structural biology." F1000Research 8 (February 22, 2019): 211. http://dx.doi.org/10.12688/f1000research.16234.1.

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Innovations are expanding the capabilities of experimental investigations of the structural properties of membrane proteins. Traditionally, three-dimensional structures have been determined by measuring x-ray diffraction using protein crystals with a size of least 100 μm. For membrane proteins, achieving crystals suitable for these measurements has been a significant challenge. The availabilities of micro-focus x-ray beams and the new instrumentation of x-ray free-electron lasers have opened up the possibility of using submicrometer-sized crystals. In addition, advances in cryo-electron micros

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34

Thunnissen, M. G. M. Marjolein, Peet A. Franken, Gerard H. de Haas, et al. "Site-directed mutagenesis and X-ray crystallography of two phospholipase A2 mutants: Y52F and Y73F." "Protein Engineering, Design and Selection" 5, no. 7 (1992): 597–603. http://dx.doi.org/10.1093/protein/5.7.597.

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35

Violante, A., A. de Cristofaro, M. A. Rao, and L. Gianfreda. "Physicochemical properties of protein-smectite and protein-Al(OH)x-smectite complexes." Clay Minerals 30, no. 4 (1995): 325–36. http://dx.doi.org/10.1180/claymin.1995.030.4.06.

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AbstractProteins (catalase, albumin, pepsin and lysozyme with different molecular weights and isoelectric points) were differently adsorbed at pH 7.0 on the clay fraction of three raw Na-saturated smectites (Crook and Uri montmorillonites and one hectorite). The adsorption isotherms of proteins on clay minerals showed typical Langmuir characteristics. Lysozyme was adsorbed under the effect of electrostatic interactions between the opposite charges of clay surfaces and protein molecules, whereas catalase and albumin were adsorbed under the effect of non-electrostatic forces. Pepsin was held in

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36

Bacellar, Camila, Dominik Kinschel, Giulia F. Mancini, et al. "Spin cascade and doming in ferric hemes: Femtosecond X-ray absorption and X-ray emission studies." Proceedings of the National Academy of Sciences 117, no. 36 (2020): 21914–20. http://dx.doi.org/10.1073/pnas.2009490117.

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The structure–function relationship is at the heart of biology, and major protein deformations are correlated to specific functions. For ferrous heme proteins, doming is associated with the respiratory function in hemoglobin and myoglobins. Cytochromec(Cyt c) has evolved to become an important electron-transfer protein in humans. In its ferrous form, it undergoes ligand release and doming upon photoexcitation, but its ferric form does not release the distal ligand, while the return to the ground state has been attributed to thermal relaxation. Here, by combining femtosecond Fe Kαand KβX-ray em

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37

Poenisch, Marion, Gunhild Unterstab, Thorsten Wolff, Peter Staeheli, and Urs Schneider. "The X protein of Borna disease virus regulates viral polymerase activity through interaction with the P protein." Journal of General Virology 85, no. 7 (2004): 1895–98. http://dx.doi.org/10.1099/vir.0.80002-0.

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Borna disease virus polymerase activity is negatively regulated by the viral X protein. Using a virus minireplicon system it was found that all X mutants that no longer interacted with the viral P protein failed to exhibit significant inhibitory activity. The action of X could further be neutralized by expression of a P fragment that contained the X interaction domain but lacked all domains known to mediate interaction with other viral proteins. X thus appears to regulate the activity of the Borna disease virus polymerase by targeting the polymerase cofactor P.

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38

Wood, Jonny, Robert M. Frederickson, Stanley Fields, and Arvind H. Patel. "Hepatitis C Virus 3′X Region Interacts with Human Ribosomal Proteins." Journal of Virology 75, no. 3 (2001): 1348–58. http://dx.doi.org/10.1128/jvi.75.3.1348-1358.2001.

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ABSTRACT To identify proteins that can bind the 3′ untranslated region (UTR) of hepatitis C virus (HCV) we screened human cDNA libraries using theSaccharomyces cerevisiae three-hybrid system. Screening with an RNA sequence derived from the 3′-terminal 98 nucleotides (3′X region) of an infectious clone of HCV (H77c) yielded clones of human ribosomal proteins L22, L3, S3, and mL3, a mitochondrial homologue of L3. We performed preliminary characterization of the binding between the 3′X region and these proteins by a three-hybrid mating assay using mutant 3′X sequences. We have further characteriz

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39

Peeters, Ben, Paul Verbruggen, Frank Nelissen, and Olav de Leeuw. "The P gene of Newcastle disease virus does not encode an accessory X protein." Journal of General Virology 85, no. 8 (2004): 2375–78. http://dx.doi.org/10.1099/vir.0.80160-0.

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Many paramyxoviruses encode non-essential accessory proteins that are involved in the regulation of virus replication and inhibition of cellular antiviral responses. It has been suggested that the P gene mRNA of Newcastle disease virus (NDV) encodes an accessory protein – the so-called X protein – by translation initiation at a conserved in-frame AUG codon at position 120. Using a monoclonal antibody that specifically detected the P and X proteins, it was shown that an accessory X protein was not expressed in NDV-infected cells. Recombinant NDV strains in which the AUG was changed into a GCC (

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40

Jenne, Dieter, Ferdinand Hugo, and Sucharit Bhakdi. "Monoclonal antibodies to human plasma Protein X alias complement S-protein." Bioscience Reports 5, no. 4 (1985): 343–52. http://dx.doi.org/10.1007/bf01116907.

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Protein X alias complement S-protein was isolated by dissociation from purified XCSb-9 (fluid-phase terminal C5b-9) complexes with 250 mM deoxycholate and subsequent sucrose density gradient centrifugation and Sephacryl gel chromatography. Polyclonal rabbit and monoclonal mouse antibodies were used to preliminarily characterize the protein in human serum and plasma. In plasma, Protein X yielded a symmetrical immuno-precipitate of α2-mobility in a crossed immunoelectrophoresis assay. However, a second immunoprecipitate of Oh-mobility was observed when serum was analysed; this precipitate repres

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41

Shofa, Maya, Yuri V. Fukushima, and Akatsuki Saito. "Conserved Yet Divergent Smc5/6 Complex Degradation by Mammalian Hepatitis B Virus X Proteins." International Journal of Molecular Sciences 26, no. 14 (2025): 6786. https://doi.org/10.3390/ijms26146786.

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Hepatitis B virus (HBV), belonging to the genus Orthohepadnavirus, can cause chronic hepatitis and hepatocarcinoma in humans. HBV ensures optimal replication by encoding X, a multifunctional protein responsible for degrading the structural maintenance of chromosomes (Smc) 5/6 complex, an anti-HBV factor in hepatocytes. Previous studies suggest that degradation of the Smc5/6 complex is conserved among viruses from the genus Orthohepadnavirus. Recently, a novel hepadnavirus in cats, domestic cat HBV (DCHBV), has been identified as genetically close to HBV. However, it remains unclear whether the

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42

Lipfert, Jan, and Sebastian Doniach. "Small-Angle X-Ray Scattering from RNA, Proteins, and Protein Complexes." Annual Review of Biophysics and Biomolecular Structure 36, no. 1 (2007): 307–27. http://dx.doi.org/10.1146/annurev.biophys.36.040306.132655.

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43

Chen, Wei Ning. "HBV X protein interacts with cytoskeletal signaling proteins through SH3 binding." Frontiers in Bioscience E2, no. 1 (2010): 143–50. http://dx.doi.org/10.2741/e76.

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44

Gavel, Ylva, and Gunnar von Heijne. "Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering." "Protein Engineering, Design and Selection" 3, no. 5 (1990): 433–42. http://dx.doi.org/10.1093/protein/3.5.433.

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45

Madhusudan and M. Vijayan. "Additional binding sites in lysozyme. X-ray analysis of lysozyme complexes with bromophenol red and bromophenol blue." "Protein Engineering, Design and Selection" 5, no. 5 (1992): 399–404. http://dx.doi.org/10.1093/protein/5.5.399.

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46

Kim, Youngsoo, and Jon D. Robertus. "Analysis of several key active site residues of ricin A chain by mutagenesis and X-ray crystallography." "Protein Engineering, Design and Selection" 5, no. 8 (1992): 775–79. http://dx.doi.org/10.1093/protein/5.8.775.

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47

Lawson, David M., Andrzej M. Brzozowski, Stephane Rety, Chandra Verma, and G. Guy Dodson. "Probing the nature of substrate binding in Humicola lanuginosa lipase through X-ray crystallography and intuitive modelling." "Protein Engineering, Design and Selection" 7, no. 4 (1994): 543–50. http://dx.doi.org/10.1093/protein/7.4.543.

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48

Greenough, W. T., A. Y. Klintsova, S. A. Irwin, R. Galvez, K. E. Bates, and I. J. Weiler. "Synaptic regulation of protein synthesis and the fragile X protein." Proceedings of the National Academy of Sciences 98, no. 13 (2001): 7101–6. http://dx.doi.org/10.1073/pnas.141145998.

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49

Colip, Leslie A., Andrew T. Koppisch, Richard D. Broene, et al. "A rapid method for quantifying heavy atom derivatives for multiple isomorphous replacement in protein crystallography." Journal of Applied Crystallography 42, no. 2 (2009): 329–32. http://dx.doi.org/10.1107/s0021889809000077.

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A rapid and simple X-ray fluorescence-based method is reported for characterizing heavy atom derivatives of proteins for protein crystallography using multiple isomorphous replacement (MIR). MIR is a widely used technique for solving protein crystallographic structures which requires that a `heavy atom' be incorporated into the protein to provide a strong signal in the diffraction pattern. Current methods for determining the effectiveness of these protein–heavy atom reactions are not always successful. In contrast, X-ray fluorescence quickly determines the presence of heavy atom modifications

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50

TAMANINI, Filippo, Leontine VAN UNEN, Cathy BAKKER, et al. "Oligomerization properties of fragile-X mental-retardation protein (FMRP) and the fragile-X-related proteins FXR1P and FXR2P." Biochemical Journal 343, no. 3 (1999): 517–23. http://dx.doi.org/10.1042/bj3430517.

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The absence of fragile-X mental-retardation protein (FMRP) results in fragile-X syndrome. Two other fragile-X-related (FXR) proteins have been described, FXR1P and FXR2P, which are both very similar in amino acid sequence to FMRP. Interaction between the three proteins as well as with themselves has been demonstrated. The FXR proteins are believed to play a role in RNA metabolism. To characterize a possible functional role of the interacting proteins the complex formation of the FXR proteins was studied in mammalian cells. Double immunofluorescence analysis in COS cells over-expressing either

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