scholarly journals Identification and characterization of the role of c-terminal Src kinase in dengue virus replication

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Rinki Kumar ◽  
Tanvi Agrawal ◽  
Naseem Ahmed Khan ◽  
Yuji Nakayama ◽  
Guruprasad R. Medigeshi
Keyword(s):  
Dengue Virus ◽  
Virus Replication ◽  
Src Kinase ◽  
Identification And Characterization

Identification and Characterization of Early Genes Involved in Epstein-Barr Virus Replication

1987 ◽  
pp. 193-194
Author(s):  
C. X. Zhang ◽  
M. Tessier ◽  
G. Decaussin ◽  
J. Daillie ◽  
T. Ooka
Keyword(s):  
Virus Replication ◽  
Epstein Barr Virus ◽  
Barr Virus ◽  
Early Genes ◽  
Epstein Barr ◽  
Identification And Characterization

scholarly journals Characterization of RyDEN (C19orf66) as an Interferon-Stimulated Cellular Inhibitor against Dengue Virus Replication

2016 ◽  
Vol 12 (1) ◽  
pp. e1005357 ◽  
Author(s):  
Youichi Suzuki ◽  
Wei-Xin Chin ◽  
Qi'En Han ◽  
Koji Ichiyama ◽  
Ching Hua Lee ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Virus Replication

scholarly journals 85: Identification and characterization of an original mechanism of resistance to gefitinib in non-small lung cancers: role of amphiregulin

2010 ◽  
Vol 97 (1) ◽  
pp. S70-S71
Author(s):  
Busser Benoît ◽  
Lucie Sancey ◽  
Véronique Josserand ◽  
Saadi Khochbin ◽  
Jean-Luc Coll ◽  
...  
Keyword(s):  
Lung Cancers ◽  
Mechanism Of Resistance ◽  
Identification And Characterization

Identification and characterization of cauliflower mosaic virus replication complexes—Analogy to hepatitis B viruses

Virology ◽  
1985 ◽  
Vol 143 (1) ◽  
pp. 212-223 ◽  
Author(s):  
Loren Marsh ◽  
Ann Kuzj ◽  
Tom Guilfoyle
Keyword(s):  
Hepatitis B ◽  
Mosaic Virus ◽  
Virus Replication ◽  
Cauliflower Mosaic Virus ◽  
Identification And Characterization

scholarly journals Identification and characterization of host proteins bound to dengue virus 3′ UTR reveal an antiviral role for quaking proteins

RNA ◽  
2018 ◽  
Vol 24 (6) ◽  
pp. 803-814 ◽  
Author(s):  
Kuo-Chieh Liao ◽  
Vanessa Chuo ◽  
Wy Ching Ng ◽  
Suat Peng Neo ◽  
Julien Pompon ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Host Proteins ◽  
Antiviral Role ◽  
Identification And Characterization

scholarly journals Insight into the essential role of the Helicobacter pylori HP1043 orphan response regulator: genome-wide identification and characterization of the DNA-binding sites

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Simone Pelliciari ◽  
Eva Pinatel ◽  
Andrea Vannini ◽  
Clelia Peano ◽  
Simone Puccio ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Binding Sites ◽  
Essential Role ◽  
Response Regulator ◽  
Dna Binding Sites ◽  
Genome Wide ◽  
Identification And Characterization ◽  
Insight Into

Identification and Characterization of Carbohydrate Molecules in Mammalian Cells Recognized by Dengue Virus Type 2

2006 ◽  
Vol 139 (3) ◽  
pp. 607-614 ◽  
Author(s):  
Chie Aoki ◽  
Kazuya I.P.J. Hidari ◽  
Saki Itonori ◽  
Akihiro Yamada ◽  
Naonori Takahashi ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Virus Type ◽  
Mammalian Cells ◽  
Identification And Characterization ◽  
Dengue Virus Type 2

scholarly journals A small mitochondrial protein present in myzozoans is essential for malaria transmission

Open Biology ◽  
2016 ◽  
Vol 6 (4) ◽  
pp. 160034 ◽  
Author(s):  
Dennis Klug ◽  
Gunnar R. Mair ◽  
Friedrich Frischknecht ◽  
Ross G. Douglas
Keyword(s):  
Drug Targets ◽  
Mitochondrial Protein ◽  
Sister Group ◽  
Developmental Defect ◽  
Mitochondrial Mass ◽  
First Time ◽  
Potential Drug Targets ◽  
Identification And Characterization

Myzozoans (which include dinoflagellates, chromerids and apicomplexans) display notable divergence from their ciliate sister group, including a reduced mitochondrial genome and divergent metabolic processes. The factors contributing to these divergent processes are still poorly understood and could serve as potential drug targets in disease-causing protists. Here, we report the identification and characterization of a small mitochondrial protein from the rodent-infecting apicomplexan parasite Plasmodium berghei that is essential for development in its mosquito host. Parasites lacking the gene mitochondrial protein ookinete developmental defect ( mpodd ) showed malformed parasites that were unable to transmit to mosquitoes. Knockout parasites displayed reduced mitochondrial mass without affecting organelle integrity, indicating no role of the protein in mitochondrial biogenesis or morphology maintenance but a likely role in mitochondrial import or metabolism. Using genetic complementation experiments, we identified a previously unrecognized Plasmodium falciparum homologue that can rescue the mpodd(−) phenotype, thereby showing that the gene is functionally conserved. As far as can be detected, mpodd is found in myzozoans, has homologues in the phylum Apicomplexa and appears to have arisen in free-living dinoflagellates. This suggests that the MPODD protein has a conserved mitochondrial role that is important for myzozoans. While previous studies identified a number of essential proteins which are generally highly conserved evolutionarily, our study identifies, for the first time, a non-canonical protein fulfilling a crucial function in the mitochondrion during parasite transmission.

scholarly journals Identification and Characterization of the Penicillin-Binding Protein 2a of Streptococcus pneumoniae and Its Possible Role in Resistance to β-Lactam Antibiotics

2000 ◽  
Vol 44 (6) ◽  
pp. 1745-1748 ◽  
Author(s):  
Genshi Zhao ◽  
Timothy I. Meier ◽  
Joann Hoskins ◽  
Kelly A. McAllister
Keyword(s):  
Streptococcus Pneumoniae ◽  
Binding Protein ◽  
Penicillin Resistance ◽  
Penicillin Binding Protein ◽  
Insertional Mutant ◽  
Identification And Characterization

ABSTRACT To further understand the role of penicillin-binding protein 2a (PBP 2a) of Streptococcus pneumoniae in penicillin resistance, we confirmed the identity of the protein as PBP 2a. The PBP 2a protein migrated electrophoretically to a position corresponding to that of PBP 2x, PBP 2a, and PBP 2b of S. pneumoniae and was absent in a pbp2ainsertional mutant of S. pneumoniae. We found that the affinities of PBP 2a for penicillins were lower than for cephalosporins and a carbapenem. When compared with other S. pneumoniae PBPs, PBP 2a exhibited lower affinities for β-lactam antibiotics, especially penicillins. Therefore, PBP 2a is a low-affinity PBP for β-lactam antibiotics in S. pneumoniae.

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