다음과 같은 기능을 한번의 로그인으로 사용 할 수 있습니다.
NTIS 바로가기
Philosophical transactions. Biological sciences, v.373 no.1738, 2018년, pp.20160523 - 20160523
Jeffery, Constance J. (Department of Biological Sciences, University of Illinois at Chicago, , Chicago, IL 60607, USA)
AI-Helper
Members of the GroEL/HSP60 protein family have been studied for many years because of their critical roles as ATP-dependent molecular chaperones, so it might come as a surprise that some have important functions in ATP-poor conditions, for example, when secreted outside the cell. At least some membe...
Jeffery, Constance J.. Moonlighting proteins. Trends in biochemical sciences, vol.24, no.1, 8-11.
Mani, Mathew, Chen, Chang, Amblee, Vaishak, Liu, Haipeng, Mathur, Tanu, Zwicke, Grant, Zabad, Shadi, Patel, Bansi, Thakkar, Jagravi, Jeffery, Constance J.. MoonProt: a database for proteins that are known to moonlight. Nucleic acids research, vol.43, no.d1, D277-D282.
Hendriks, W, Mulders, J W, Bibby, M A, Slingsby, C, Bloemendal, H, de Jong, W W. Duck lens epsilon-crystallin and lactate dehydrogenase B4 are identical: a single-copy gene product with two distinct functions.. Proceedings of the National Academy of Sciences of the United States of America, vol.85, no.19, 7114-7118.
PIATIGORSKY, JORAM. Multifunctional Lens Crystallins and Corneal Enzymes: More than Meets the Eye. Annals of the New York Academy of Sciences, vol.842, no.1, 7-15.
Wistow, Graeme J., Mulders, John W. M., de Jong, Wilfried W.. The enzyme lactate dehydrogenase as a structural protein in avian and crocodilian lenses. Nature, vol.326, no.6113, 622-624.
J. Biol. Chem. Rao PV 96 267 1992 10.1016/S0021-9258(18)48464-5 Identification and characterization of the enzymatic activity of zeta-crystallin from guinea pig lens. A novel NADPH:quinone oxidoreductase
Rao, P.Vasantha, Zigler Jr., J.Samuel. Extremely high levels of NADPH in guinea pig lens: Correlation with zeta-crystallin concentration. Biochemical and biophysical research communications, vol.167, no.3, 1221-1228.
Huang, Q.-L., Russell, P., Stone, S. H., Zigler, J. S.. Zeta-crystallin, a novel lens protein from the guinea pig. Current eye research, vol.6, no.5, 725-732.
Bateman, O. A., Purkiss, A. G., van Montfort, R., Slingsby, C., Graham, C., Wistow, G.. Crystal Structure of &eegr;-Crystallin: Adaptation of a Class 1 Aldehyde Dehydrogenase for a New Role in the Eye Lens. Biochemistry, vol.42, no.15, 4349-4356.
Banerjee, Sharmistha, Nandyala, Ashok Kumar, Raviprasad, Podili, Ahmed, Niyaz, Hasnain, Seyed E.. Iron-Dependent RNA-Binding Activity of Mycobacterium tuberculosis Aconitase. Journal of bacteriology, vol.189, no.11, 4046-4052.
Kennedy, M C, Mende-Mueller, L, Blondin, G A, Beinert, H. Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein.. Proceedings of the National Academy of Sciences of the United States of America, vol.89, no.24, 11730-11734.
Philpott, C C, Klausner, R D, Rouault, T A. The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation.. Proceedings of the National Academy of Sciences of the United States of America, vol.91, no.15, 7321-7325.
A major surface protein on group A streptococci is a glyceraldehyde-3- phosphate-dehydrogenase with multiple binding activity. The Journal of experimental medicine, vol.176, no.2, 415-426.
Infect. Immun. Gozalbo D 2052 66 1998 10.1128/IAI.66.5.2052-2059.1998 The cell wall-associated glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is also a fibronectin and laminin binding protein
Matta, Sumit Kumar, Agarwal, Shivangi, Bhatnagar, Rakesh. Surface localized and extracellular Glyceraldehyde-3-phosphate dehydrogenase of Bacillus anthracis is a plasminogen binding protein. Biochimica et biophysica acta. Proteins and proteomics, vol.1804, no.11, 2111-2120.
Int. Microbiol. Aguilera L 187 12 2009 NAD+-dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase
Hurmalainen, Veera, Edelman, Sanna, Antikainen, Jenni, Baumann, Marc, Lähteenmäki, Kaarina, Korhonen, Timo K. Extracellular proteins of Lactobacillus crispatus enhance activation of human plasminogen. Microbiology, vol.153, no.4, 1112-1122.
Kinoshita, H., Uchida, H., Kawai, Y., Kawasaki, T., Wakahara, N., Matsuo, H., Watanabe, M., Kitazawa, H., Ohnuma, S., Miura, K., Horii, A., Saito, T.. Cell surface Lactobacillus plantarum LA 318 glyceraldehyde-3-phosphate dehydrogenase (GAPDH) adheres to human colonic mucin. Journal of applied microbiology, vol.104, no.6, 1667-1674.
Alvarez, René A., Blaylock, Mark W., Baseman, Joel B.. Surface localized glyceraldehyde-3-phosphate dehydrogenase of Mycoplasma genitalium binds mucin. Molecular microbiology, vol.48, no.5, 1417-1425.
Tunio, Sarfraz A, Oldfield, Neil J, Ala'Aldeen, Dlawer AA, Wooldridge, Karl G, Turner, David PJ. The role of glyceraldehyde 3-phosphate dehydrogenase (GapA-1) in Neisseria meningitidis adherence to human cells. BMC microbiology, vol.10, 280-280.
Barbosa, Mônica Santiago, Báo, Sônia Nair, Andreotti, Patrícia Ferrari, de Faria, Fabrícia P., Felipe, Maria Sueli S., dos Santos Feitosa, Luciano, Mendes-Giannini, Maria José Soares, de Almeida Soares, Célia Maria. Glyceraldehyde-3-Phosphate Dehydrogenase of Paracoccidioides brasiliensis Is a Cell Surface Protein Involved in Fungal Adhesion to Extracellular Matrix Proteins and Interaction with Cells. Infection and immunity, vol.74, no.1, 382-389.
Infect. Immun. Modun B 1086 67 1999 10.1128/IAI.67.3.1086-1092.1999 The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase
Winram, S. B., Lottenberg, R.. The plasmin-binding protein Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase. Microbiology, vol.142, no.8, 2311-2320.
J. Microbiol. Seifert KN 350 49 2003 Characterization of group B streptococcal glyceraldehyde-3-phosphate dehydrogenase: surface localization, enzymatic activity, and protein-protein interactions
Bergmann, Simone, Rohde, Manfred, Hammerschmidt, Sven. Glyceraldehyde-3-Phosphate Dehydrogenase of Streptococcus pneumoniae Is a Surface-Displayed Plasminogen-Binding Protein. Infection and immunity, vol.72, no.4, 2416-2419.
Jin, Hong, Song, Youngmia P., Boel, Gregory, Kochar, Jaspreet, Pancholi, Vijay. Group A Streptococcal Surface GAPDH, SDH, Recognizes uPAR/CD87 as its Receptor on the Human Pharyngeal Cell and Mediates Bacterial Adherence to Host Cells. Journal of molecular biology, vol.350, no.1, 27-41.
Jobin, Marie-Claude, Brassard, Julie, Quessy, Sylvain, Gottschalk, Marcelo, Grenier, Daniel. Acquisition of Host Plasmin Activity by the Swine PathogenStreptococcus suisSerotype 2. Infection and immunity, vol.72, no.1, 606-610.
Lama, A., Kucknoor, A., Mundodi, V., Alderete, J. F.. Glyceraldehyde-3-Phosphate Dehydrogenase Is a Surface-Associated, Fibronectin-Binding Protein of Trichomonas vaginalis. Infection and immunity, vol.77, no.7, 2703-2711.
Boone, Tyler J., Burnham, Carey-Ann D., Tyrrell, Gregory J.. Binding of group B streptococcal phosphoglycerate kinase to plasminogen and actin. Microbial pathogenesis, vol.51, no.4, 255-261.
Thromb. Haemost. Fulde M 401 111 2013 Pneumococcal phosphoglycerate kinase interacts with plasminogen and its tissue activator
Bergmann, S., Schoenen, H., Hammerschmidt, S.. The interaction between bacterial enolase and plasminogen promotes adherence of Streptococcus pneumoniae to epithelial and endothelial cells. International journal of medical microbiology : IJMM, vol.303, no.8, 452-462.
Bergmann, Simone, Rohde, Manfred, Chhatwal, Gursharan S., Hammerschmidt, Sven. &agr;-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Molecular microbiology, vol.40, no.6, 1273-1287.
Bergmann, Simone, Wild, Daniela, Diekmann, Oliver, Frank, Ronald, Bracht, Dagmar, Chhatwal, Gursharan S., Hammerschmidt, Sven. Identification of a novel plasmin(ogen)-binding motif in surface displayed &agr;-enolase of Streptococcus pneumoniae. Molecular microbiology, vol.49, no.2, 411-423.
Indian J. Med. Res. Bergmann S 29 119 2004 Characterization of plasmin(ogen) binding to Streptococcus pneumoniae
Sha, Jian, Erova, Tatiana E., Alyea, Rebecca A., Wang, Shaofei, Olano, Juan P., Pancholi, Vijay, Chopra, Ashok K.. Surface-Expressed Enolase Contributes to the Pathogenesis of Clinical Isolate SSU ofAeromonas hydrophila. Journal of bacteriology, vol.191, no.9, 3095-3107.
Agarwal, S., Kulshreshtha, P., Bambah Mukku, D., Bhatnagar, R.. α-Enolase binds to human plasminogen on the surface of Bacillus anthracis. Biochimica et biophysica acta. Proteins and proteomics, vol.1784, no.7, 986-994.
Candela, Marco, Biagi, Elena, Centanni, Manuela, Turroni, Silvia, Vici, Manuela, Musiani, Francesco, Vitali, Beatrice, Bergmann, Simone, Hammerschmidt, Sven, Brigidi, Patrizia. Bifidobacterial enolase, a cell surface receptor for human plasminogen involved in the interaction with the host. Microbiology, vol.155, no.10, 3294-3303.
Floden, Angela M., Watt, John A., Brissette, Catherine A.. Borrelia burgdorferi Enolase Is a Surface-Exposed Plasminogen Binding Protein. PloS one, vol.6, no.11, e27502-.
Jong, Ambrose Y., Chen, Steven H. M., Stins, Monique F., Kim, Kwang Sik, Tuan, Tan-Lan, Huang, Sheng-He. Binding of Candida albicans enolase to plasmin(ogen) results in enhanced invasion of human brain microvascular endothelial cells. Journal of medical microbiology, vol.52, no.8, 615-622.
Miles, Lindsey A., Dahlberg, Carol M., Plescia, Janet, Felez, Jordi, Kato, Kanefusa, Plow, Edward F.. Role of cell-surface lysines in plasminogen binding to cells: identification of .alpha.-enolase as a candidate plasminogen receptor. Biochemistry, vol.30, no.6, 1682-1691.
Redlitz, Alexander, Fowler, Bruce J., Plow, Edward F., Miles, Lindsey A.. The Role of an Enolase‐Related Molecule in Plasminogen Binding to Cells. European journal of biochemistry, vol.227, no.1, 407-415.
Vanegas, Gilmer, Quiñones, Wilfredo, Carrasco-López, Cesar, Concepción, Juan Luis, Albericio, Fernando, Avilán, Luisana. Enolase as a plasminogen binding protein in Leishmania mexicana. Parasitology research, vol.101, no.6, 1511-1516.
Jolodar, Abbas, Fischer, Peter, Bergmann, Simone, Büttner, Dietrich W., Hammerschmidt, Sven, Brattig, Norbert W.. Molecular cloning of an α-enolase from the human filarial parasite Onchocerca volvulus that binds human plasminogen. Biochimica et biophysica acta. Gene structure and expression, vol.1627, no.2, 111-120.
Donofrio, Fabiana Cristina, Calil, Ana Carolina Alvarez, Miranda, Elaine Toscano, Almeida, Ana Marisa Fusco, Benard, Gil, Soares, Christiane Pienna, Veloso, Sarah Nogueira, Soares, Célia Maria de Almeida, Mendes Giannini, Maria José Soares. Enolase from Paracoccidioides brasiliensis: isolation and identification as a fibronectin-binding protein. Journal of medical microbiology, vol.58, no.6, 706-713.
Nakajima, Kazuyuki, Hamanoue, Makoto, Takemoto, Nagisa, Hattori, Tatsuya, Kato, Kanefusa, Kohsaka, Shinichi. Plasminogen Binds Specifically to α‐Enolase on Rat Neuronal Plasma Membrane. Journal of neurochemistry, vol.63, no.6, 2048-2057.
de la Torre-Escudero, E., Manzano-Roman, R., Perez-Sanchez, R., Siles-Lucas, M., Oleaga, A.. Cloning and characterization of a plasminogen-binding surface-associated enolase from Schistosoma bovis. Veterinary parasitology, vol.173, no.1, 76-84.
Carneiro, Celia R.W., Postol, Edilberto, Nomizo, Regina, Reis, Luiz F.L., Brentani, Ricardo R.. Identification of enolase as a laminin-binding protein on the surface of Staphylococcus aureus. Microbes and infection, vol.6, no.6, 604-608.
Kinnby, Bertil, Booth, Nuala A., Svensäter, Gunnel. Plasminogen binding by oral streptococci from dental plaque and inflammatory lesions. Microbiology, vol.154, no.3, 924-931.
Jones, Micheala N., Holt, Robert G.. Cloning and characterization of an α-enolase of the oral pathogen Streptococcus mutans that binds human plasminogen. Biochemical and biophysical research communications, vol.364, no.4, 924-929.
Kolberg, Jan, Aase, Audun, Bergmann, Simone, Herstad, Tove K., Rødal, Gunnhild, Frank, Ronald, Rohde, Manfred, Hammerschmidt, Sven. Streptococcus pneumoniae enolase is important for plasminogen binding despite low abundance of enolase protein on the bacterial cell surface. Microbiology, vol.152, no.5, 1307-1317.
Antikainen, Jenni, Kuparinen, Veera, Lähteenmäki, Kaarina, Korhonen, Timo K.. Enolases from Gram-positive bacterial pathogens and commensal lactobacilli share functional similarity in virulence-associated traits : Functions of bacterial enolases. FEMS immunology and medical microbiology, vol.51, no.3, 526-534.
Castaldo, Cristiana, Vastano, Valeria, Siciliano, Rosa Anna, Candela, Marco, Vici, Manuela, Muscariello, Lidia, Marasco, Rosangela, Sacco, Margherita. Surface displaced alfa-enolase of Lactobacillus plantarum is a fibronectin binding protein. Microbial cell factories, vol.8, 14-14.
Pancholi, Vijaykumar, Fischetti, Vincent A.. α-Enolase, a Novel Strong Plasmin(ogen) Binding Protein on the Surface of Pathogenic Streptococci. The Journal of biological chemistry, vol.273, no.23, 14503-14515.
Esgleas, Miriam, Li, Yuanyi, Hancock, Mark A., Harel, Josée, Dubreuil, J. Daniel, Gottschalk, Marcelo. Isolation and characterization of α-enolase, a novel fibronectin-binding protein from Streptococcus suis. Microbiology, vol.154, no.9, 2668-2679.
Kim, Kwang-Pyo, Jagadeesan, Balamurugan, Burkholder, Kristin M., Jaradat, Ziad W., Wampler, Jennifer L., Lathrop, Amanda A., Morgan, Mark T., Bhunia, Arun K.. Adhesion characteristics of Listeria adhesion protein (LAP)-expressing Escherichia coli to Caco-2 cells and of recombinant LAP to eukaryotic receptor Hsp60 as examined in a surface plasmon resonance sensor : Adhesion characteristics of LAP. FEMS microbiology letters, vol.256, no.2, 324-332.
Wampler, Jennifer L., Kim, Kwang-Pyo, Jaradat, Ziad, Bhunia, Arun K.. Heat Shock Protein 60 Acts as a Receptor for theListeriaAdhesion Protein in Caco-2 Cells. Infection and immunity, vol.72, no.2, 931-936.
Burkholder, Kristin M., Bhunia, Arun K.. Listeria monocytogenes Uses Listeria Adhesion Protein (LAP) To Promote Bacterial Transepithelial Translocation and Induces Expression of LAP Receptor Hsp60. Infection and immunity, vol.78, no.12, 5062-5073.
Candela, Marco, Centanni, Manuela, Fiori, Jessica, Biagi, Elena, Turroni, Silvia, Orrico, Catia, Bergmann, Simone, Hammerschmidt, Sven, Brigidi, Patrizia. DnaK from Bifidobacterium animalis subsp. lactis is a surface-exposed human plasminogen receptor upregulated in response to bile salts. Microbiology, vol.156, no.6, 1609-1618.
Dallo, Shatha F., Kannan, T. R., Blaylock, Mark W., Baseman, Joel B.. Elongation factor Tu and E1 &bgr; subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae. Molecular microbiology, vol.46, no.4, 1041-1051.
Kunert, Anja, Losse, Josephine, Gruszin, Christin, Hühn, Michael, Kaendler, Kerstin, Mikkat, Stefan, Volke, Daniela, Hoffmann, Ralf, Jokiranta, T. Sakari, Seeberger, Harald, Moellmann, Ute, Hellwage, Jens, Zipfel, Peter F.. Immune Evasion of the Human Pathogen Pseudomonas aeruginosa: Elongation Factor Tuf Is a Factor H and Plasminogen Binding Protein. The journal of immunology : official journal of the American Association of Immunologists, vol.179, no.5, 2979-2988.
Granato, Dominique, Bergonzelli, Gabriela E., Pridmore, Raymond David, Marvin, Laure, Rouvet, Martine, Corthésy-Theulaz, Irène E.. Cell Surface-Associated Elongation Factor Tu Mediates the Attachment of Lactobacillus johnsonii NCC533 (La1) to Human Intestinal Cells and Mucins. Infection and immunity, vol.72, no.4, 2160-2169.
Brix, K, Summa, W, Lottspeich, F, Herzog, V. Extracellularly occurring histone H1 mediates the binding of thyroglobulin to the cell surface of mouse macrophages.. The Journal of clinical investigation, vol.102, no.2, 283-293.
10.1093/nar/18.10.3054
Kumar, S., Sheokand, N., Mhadeshwar, M.A., Raje, C.I., Raje, M.. Characterization of glyceraldehyde-3-phosphate dehydrogenase as a novel transferrin receptor. The international journal of biochemistry & cell biology, vol.44, no.1, 189-199.
Bocharov, Alexander V., Vishnyakova, Tatyana G., Baranova, Irina N., Remaley, Alan T., Patterson, Amy P., Eggerman, Thomas L.. Heat Shock Protein 60 Is a High-Affinity High-Density Lipoprotein Binding Protein. Biochemical and biophysical research communications, vol.277, no.1, 228-235.
Petit, F.M., Serres, C., Bourgeon, F., Pineau, C., Auer, J.. Identification of sperm head proteins involved in zona pellucida binding. Human reproduction, vol.28, no.4, 852-865.
GOPALAKRISHNAN, B., ARAVINDA, S., PAWSHE, C. H., TOTEY, S. M., NAGPAL, S., SALUNKE, D. M., SHAHA, Chandrima. Studies on glutathione S-transferases important for sperm function: evidence of catalytic activity-independent functions. The Biochemical journal, vol.329, no.2, 231-241.
Auer, Jana, Camoin, Luc, Courtot, Anne-Marie, Hotellier, Françoise, De Almeida, Marta. Evidence that P36, a human sperm acrosomal antigen involved in the fertilization process is triosephosphate isomerase. Molecular reproduction and development, vol.68, no.4, 515-523.
Fulde, Marcus, Rohde, Manfred, Polok, Andy, Preissner, Klaus T., Chhatwal, Gursharan Singh, Bergmann, Simone. Cooperative Plasminogen Recruitment to the Surface of Streptococcus canis via M Protein and Enolase Enhances Bacterial Survival. mBio, vol.4, no.2, e00629-12-.
Bao, Shijun, Guo, Xiaoqin, Yu, Shengqing, Ding, Jiabo, Tan, Lei, Zhang, Fanqin, Sun, Yingjie, Qiu, Xusheng, Chen, Guanghua, Ding, Chan. Mycoplasma synoviae enolase is a plasminogen/fibronectin binding protein. BMC veterinary research, vol.10, 223-.
READ, Martin, HICKS, Karen E., SIMS, Paul F. G., HYDE, John E.. Molecular characterisation of the enolase gene from the human malaria parasite Plasmodium falciparum Evidence for ancestry within a photosynthetic lineage. European journal of biochemistry, vol.220, no.2, 513-520.
Ghosh, Anil K., Coppens, Isabelle, Gårdsvoll, Henrik, Ploug, Michael, Jacobs-Lorena, Marcelo. Plasmodium ookinetes coopt mammalian plasminogen to invade the mosquito midgut. Proceedings of the National Academy of Sciences of the United States of America, vol.108, no.41, 17153-17158.
Kesimer, Mehmet, Kiliç, Nedret, Mehrotra, Ravi, Thornton, David J, Sheehan, John K. Identification of salivary mucin MUC7 binding proteins from Streptococcus gordonii. BMC microbiology, vol.9, 163-163.
Agarwal, Vaibhav, Kuchipudi, Arunakar, Fulde, Marcus, Riesbeck, Kristian, Bergmann, Simone, Blom, Anna M.. Streptococcus pneumoniae Endopeptidase O (PepO) Is a Multifunctional Plasminogen- and Fibronectin-binding Protein, Facilitating Evasion of Innate Immunity and Invasion of Host Cells. The Journal of biological chemistry, vol.288, no.10, 6849-6863.
Sahoo, S., Murugavel, S., Devi, I. K., Vedamurthy, G. V., Gupta, S. C., Singh, B. P., Joshi, P.. Glyceraldehyde‐3‐phosphate dehydrogenase of the parasitic nematode Haemonchus contortus binds to complement C3 and inhibits its activity. Parasite immunology, vol.35, no.12, 457-467.
Knaust, Andreas, Weber, Martin V. R., Hammerschmidt, Sven, Bergmann, Simone, Frosch, Matthias, Kurzai, Oliver. Cytosolic Proteins Contribute to Surface Plasminogen Recruitment of Neisseria meningitidis. Journal of bacteriology, vol.189, no.14, 5404-5404.
Xolalpa, Wendy, Vallecillo, Antonio J., Lara, Martha, Mendoza-Hernandez, Guillermo, Comini, Marcelo, Spallek, Ralf, Singh, Mahavir, Espitia, Clara. Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis. Proteomics, vol.7, no.18, 3332-3341.
Candela, Marco, Bergmann, Simone, Vici, Manuela, Vitali, Beatrice, Turroni, Silvia, Eikmanns, Bernhard J., Hammerschmidt, Sven, Brigidi, Patrizia. Binding of Human Plasminogen toBifidobacterium. Journal of bacteriology, vol.189, no.16, 5929-5936.
Collen, D, Verstraete, M. Molecular Biology of Human Plasminogen : II. Metabolism in Physiological and Some Pathological Conditions in Man. Thrombosis et diathesis haemorrhagica, vol.34, no.2, 403-408.
10.1016/S0065-230X(08)60028-7
Patel, D.K., Shah, K.R., Pappachan, A., Gupta, S., Singh, D.D.. Cloning, expression and characterization of a mucin-binding GAPDH from Lactobacillus acidophilus. International journal of biological macromolecules, vol.91, 338-346.
FURUKAWA, TATSUHIKO, YOSHIMURA, AKIHIKO, SUMIZAWA, TOMOYUKI, HARAGUCHI, MISAKO, AKIYAMA, SHINI-ICH, FUKUI, KlYOSHI, ISHIZAWA, MlNORU, YAMADA, YUJI. Angiogenic factor. Nature, vol.356, no.6371, 668-668.
Park, Sang Gyu, Kim, Hye Jin, Min, You Hong, Choi, Eung-Chil, Shin, Young Kee, Park, Bum-Joon, Lee, Sang Won, Kim, Sunghoon. Human lysyl-tRNA synthetase is secreted to trigger proinflammatory response. Proceedings of the National Academy of Sciences of the United States of America, vol.102, no.18, 6356-6361.
J. Biol. Chem. Safer D 4029 266 1991 10.1016/S0021-9258(20)64278-8 Thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable
Cassimeris, L, Safer, D, Nachmias, V T, Zigmond, S H. Thymosin beta 4 sequesters the majority of G-actin in resting human polymorphonuclear leukocytes. The Journal of cell biology, vol.119, no.5, 1261-1270.
Safer, D., Sosnick, T. R., Elzinga, M.. Thymosin &bgr;4 Binds Actin in an Extended Conformation and Contacts both the Barbed and Pointed Ends. Biochemistry, vol.36, no.19, 5806-5816.
Young, J.D., Lawrence, A.J., MacLean, A.G., Leung, B.P., McInnes, I.B., Canas, B., Pappin, D.J.C., Stevenson, R.D.. Thymosin β 4 sulfoxide is an anti-inflammatory agent generated by monocytes in the presence of glucocorticoids. Nature medicine, vol.5, no.12, 1424-1427.
Chaput, Mariella, Claes, Victor, Portetelle, Daniel, Cludts, Isabelle, Cravador, Alfredo, Burny, Arsène, Gras, Hélène, Tartar, André. The neurotrophic factor neuroleukin is 90% homologous with phosphohexose isomerase. Nature, vol.332, no.6163, 454-455.
Faik, Pelin, Walker, James I. H., Redmill, Alison A. M., Morgan, Michael J.. Mouse glucose-6-phosphate isomerase and neuroleukin have identical 3′ sequences. Nature, vol.332, no.6163, 455-456.
Cancer Res. Watanabe H 2960 56 1996 Tumor cell autocrine motility factor is the neuroleukin/phosphohexose isomerase polypeptide
Blood Xu W 4502 87 1996 10.1182/blood.V87.11.4502.bloodjournal87114502 The differentiation and maturation mediator for human myeloid leukemia cells shares homology with neuroleukin or phosphoglucose isomerase
Gurney, ME, Heinrich, SP, Lee, MR, Yin, HS. Molecular cloning and expression of neuroleukin, a neurotrophic factor for spinal and sensory neurons. Science, vol.234, no.4776, 566-574.
Gurney, ME, Apatoff, BR, Spear, GT, Baumel, MJ, Antel, JP, Bania, MB, Reder, AT. Neuroleukin: a lymphokine product of lectin-stimulated T cells. Science, vol.234, no.4776, 574-581.
J. Biol. Chem. Watanabe H 13 442 266 1991 10.1016/S0021-9258(18)98859-9 Purification of human tumor cell autocrine motility factor and molecular cloning of its receptor
Schulz, Laura Clamon, Bahr, Janice M. Potential endocrine function of the glycolytic enzyme glucose-6-phosphate isomerase during implantation. General and comparative endocrinology, vol.137, no.3, 283-287.
Mirando, Adam C., Fang, Pengfei, Williams, Tamara F., Baldor, Linda C., Howe, Alan K., Ebert, Alicia M., Wilkinson, Barrie, Lounsbury, Karen M., Guo, Min, Francklyn, Christopher S.. Aminoacyl-tRNA synthetase dependent angiogenesis revealed by a bioengineered macrolide inhibitor. Scientific reports, vol.5, 13160-.
Querol-García, Javier, Fernández, Francisco J., Marin, Ana V., Gómez, Sara, Fullà, Daniel, Melchor-Tafur, Cecilia, Franco-Hidalgo, Virginia, Albertí, Sebastián, Juanhuix, Jordi, Rodríguez de Córdoba, Santiago, Regueiro, José R., Vega, M. Cristina. Crystal Structure of Glyceraldehyde-3-Phosphate Dehydrogenase from the Gram-Positive Bacterial Pathogen A. vaginae , an Immunoevasive Factor that Interacts with the Human C5a Anaphylatoxin. Frontiers in microbiology, vol.8, 541-.
Nandan, Devki, Tran, Thao, Trinh, Eva, Silverman, Judith M., Lopez, Martin. Identification of leishmania fructose-1,6-bisphosphate aldolase as a novel activator of host macrophage Src homology 2 domain containing protein tyrosine phosphatase SHP-1. Biochemical and biophysical research communications, vol.364, no.3, 601-607.
Nandan, Devki, Yi, Taolin, Lopez, Martin, Lai, Crystal, Reiner, Neil E.. Leishmania EF-1α Activates the Src Homology 2 Domain Containing Tyrosine Phosphatase SHP-1 Leading to Macrophage Deactivation. The Journal of biological chemistry, vol.277, no.51, 50190-50197.
Yoshida, Naofumi, Oeda, Kenji, Watanabe, Eijiro, Mikami, Toshiyuki, Fukita, Yoshikazu, Nishimura, Keiichiro, Komai, Koichiro, Matsuda, Kazuhiko. Chaperonin turned insect toxin. Nature, vol.411, no.6833, 44-44.
Liu, H., Zeng, H., Yao, Q., Yuan, J., Zhang, Y., Qiu, D., Yang, X., Yang, H., Liu, Z.. Steinernema glaseri surface enolase: Molecular cloning, biological characterization, and role in host immune suppression. Molecular and biochemical parasitology, vol.185, no.2, 89-98.
Jeffery, C. J., Bahnson, B. J., Chien, W., Ringe, D., Petsko, G. A.. Crystal Structure of Rabbit Phosphoglucose Isomerase, a Glycolytic Enzyme That Moonlights as Neuroleukin, Autocrine Motility Factor, and Differentiation Mediator,. Biochemistry, vol.39, no.5, 955-964.
Ehinger, Stefanie, Schubert, Wolf-Dieter, Bergmann, Simone, Hammerschmidt, Sven, Heinz, Dirk W.. Plasmin(ogen)-binding α-Enolase from Streptococcus pneumoniae: Crystal Structure and Evaluation of Plasmin(ogen)-binding Sites. Journal of molecular biology, vol.343, no.4, 997-1005.
Jeffery, Constance J.. Proteins with neomorphic moonlighting functions in disease. IUBMB life, vol.63, no.7, 489-494.
Kim, T.S., Kim, H.D., Kim, J.. PKCδ-dependent functional switch of rpS3 between translation and DNA repair. Biochimica et biophysica acta, Molecular cell research, vol.1793, no.2, 395-405.
Wan, Fengyi, Weaver, Amanda, Gao, Xiaofei, Bern, Michael, Hardwidge, Philip R., Lenardo, Michael J.. IKKβ phosphorylation regulates RPS3 nuclear translocation and NF-κB function during Escherichia coli O157:H7 infection. Nature immunology, vol.12, no.4, 335-343.
Carvalho, Claudine M., Santos, Anésia A., Pires, Silvana R., Rocha, Carolina S., Saraiva, Daniela I., Machado, João Paulo B., Mattos, Eliciane C., Fietto, Luciano G., Fontes, Elizabeth P. B.. Regulated Nuclear Trafficking of rpL10A Mediated by NIK1 Represents a Defense Strategy of Plant Cells against Virus. PLoS pathogens, vol.4, no.12, e1000247-.
Rocha, C.S., Santos, A.A., Machado, J.P.B., Fontes, E.P.B.. The ribosomal protein L10/QM-like protein is a component of the NIK-mediated antiviral signaling. Virology, vol.380, no.2, 165-169.
Mazumder, Barsanjit, Sampath, Prabha, Seshadri, Vasudevan, Maitra, Ratan K, DiCorleto, Paul E, Fox, Paul L. Regulated Release of L13a from the 60S Ribosomal Subunit as A Mechanism of Transcript-Specific Translational Control. Cell, vol.115, no.2, 187-198.
Adlanmerini, Marine, Solinhac, Romain, Abot, Anne, Fabre, Aurélie, Raymond-Letron, Isabelle, Guihot, Anne-Laure, Boudou, Frédéric, Sautier, Lucile, Vessières, Emilie, Kim, Sung Hoon, Lière, Philippe, Fontaine, Coralie, Krust, Andrée, Chambon, Pierre, Katzenellenbogen, John A., Gourdy, Pierre, Shaul, Philip W., Henrion, Daniel, Arnal, Jean-François, Lenfant, Françoise. Mutation of the palmitoylation site of estrogen receptor α in vivo reveals tissue-specific roles for membrane versus nuclear actions. Proceedings of the National Academy of Sciences of the United States of America, vol.111, no.2, E283-E290.
Ebner, Patrick, Rinker, Janina, Götz, Friedrich. Excretion of cytoplasmic proteins in Staphylococcus is most likely not due to cell lysis. Current genetics, vol.62, no.1, 19-23.
Ebner, Patrick, Prax, Marcel, Nega, Mulugeta, Koch, Iris, Dube, Linda, Yu, Wenqi, Rinker, Janina, Popella, Peter, Flötenmeyer, Matthias, Götz, Friedrich. Excretion of cytoplasmic proteins (ECP) in Staphylococcus aureus. Molecular microbiology, vol.97, no.4, 775-789.
Boël, Grégory, Pichereau, Vianney, Mijakovic, Ivan, Mazé, Alain, Poncet, Sandrine, Gillet, Sylvie, Giard, Jean-Christophe, Hartke, Axel, Auffray, Yanick, Deutscher, Josef. Is 2-Phosphoglycerate-dependent Automodification of Bacterial Enolases Implicated in their Export?. Journal of molecular biology, vol.337, no.2, 485-496.
Yang, C.K., Zhang, X.Z., Lu, C.D., Tai, P.C.. An internal hydrophobic helical domain of Bacillus subtilis enolase is essential but not sufficient as a non-cleavable signal for its secretion. Biochemical and biophysical research communications, vol.446, no.4, 901-905.
Daubenspeck, James M., Liu, Runhua, Dybvig, Kevin. Rhamnose Links Moonlighting Proteins to Membrane Phospholipid in Mycoplasmas. PloS one, vol.11, no.9, e0162505-.
*원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다.
출판사/학술단체 등이 한시적으로 특별한 프로모션 또는 일정기간 경과 후 접근을 허용하여, 출판사/학술단체 등의 사이트에서 이용 가능한 논문
Copyright KISTI. All Rights Reserved.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.