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Structural characterization of human Uch37.

CITE Title : Structural characterization of human Uch37. Personal Author(s) : Burgie, E. Sethe;Bingman, Craig A.;Soni, Ameet B.;Phillips, George N.; Published Date : Sep 26 2011;2-2012; Source : Proteins. 80(2):649-654 URL : https://stacks.cdc.gov/view/cdc/33291 Burgie, E. Sethe et al. (2011). Structural characterization of human Uch37.. 80(2). Burgie, E. Sethe et al. "Structural characterization of human Uch37." 80, no. 2 (2011) Burgie, E. Sethe et al. "Structural characterization of human Uch37." vol. 80, no. 2, 2011 Export RIS Citation Information.

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Burgie, E. Sethe ;

Bingman, Craig A.

Sep 26 2011 | Proteins. 80(2):649-654

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Uch37 is a de-ubiquitylating enzyme that is functionally linked with the 26S proteasome via Rpn13, and is essential for metazoan development. Here, we...
Specificity Determinants for Autoproteolysis of LexA, a Key Regulator of Bacterial SOS Mutagenesis

CITE Title : Specificity Determinants for Autoproteolysis of LexA, a Key Regulator of Bacterial SOS Mutagenesis Personal Author(s) : Mo, Charlie Y.;Birdwell, L. Dillon;Kohli, Rahul M.; Published Date : May 08 2014 Source : Biochemistry. 2014; 53(19):3158-3168. URL : https://stacks.cdc.gov/view/cdc/30743 Mo, Charlie Y. et al. (2014). Specificity Determinants for Autoproteolysis of LexA, a Key Regulator of Bacterial SOS Mutagenesis. 53(19). Mo, Charlie Y. and Birdwell, L. Dillon and Kohli, Rahul M. "Specificity Determinants for Autoproteolysis of LexA, a Key Regulator of Bacterial SOS Mutagenesis" 53, no. 19 (2014) Mo, Charlie Y. et al. "Specificity Determinants for Autoproteolysis of LexA, a Key Regulator of Bacterial SOS Mutagenesis" vol. 53, no. 19, 2014 Export RIS Citation Information.

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Mo, Charlie Y. ;

Birdwell, L. Dillon

May 08 2014 | Biochemistry. 2014; 53(19):3158-3168.

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Bacteria utilize the tightly regulated stress response (SOS) pathway to respond to a variety of genotoxic agents, including antimicrobials. Activation...
Targeted disruption of DNMT1, DNMT3A and DNMT3B in human embryonic stem cells

CITE Title : Targeted disruption of DNMT1, DNMT3A and DNMT3B in human embryonic stem cells Personal Author(s) : Liao, Jing;Karnik, Rahul;Gu, Hongcang;Ziller, Michael J.;Clement, Kendell;Tsankov, Alexander M.;Akopian, Veronika;Gifford, Casey A.;Donaghey, Julie;Galonska, Christina;Pop, Ramona;Reyon, Deepak;Tsai, Shengdar Q.;Mallard, William;Joung, J. Keith;Rinn, John L.;Gnirke, Andreas;Meissner, Alexander; Published Date : 5 2015;5-2015; Source : Nat Genet. 47(5):469-478 URL : https://stacks.cdc.gov/view/cdc/31723 Liao, Jing et al. (2015). Targeted disruption of DNMT1, DNMT3A and DNMT3B in human embryonic stem cells. 47(5). Liao, Jing et al. "Targeted disruption of DNMT1, DNMT3A and DNMT3B in human embryonic stem cells" 47, no. 5 (2015) Liao, Jing et al. "Targeted disruption of DNMT1, DNMT3A and DNMT3B in human embryonic stem cells" vol. 47, no. 5, 2015 Export RIS Citation Information.

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Liao, Jing ;

Karnik, Rahul

5 2015 | Nat Genet. 47(5):469-478

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DNA methylation is a key epigenetic modification involved in regulating gene expression and maintaining genomic integrity. Here we inactivated all thr...
Structural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase: the role of tryptophan 93 in ligand orientation

CITE Title : Structural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase: the role of tryptophan 93 in ligand orientation Personal Author(s) : Inoguchi, Noriko;Chaiseeda, Kittichai;Yamanishi, Mamoru;Kim, Moon Ki;Jang, Yunho;Bajaj, Mamta;Chia, Catherine P.;Becker, Donald F.;Moriyama, Hideaki; Published Date : Dec 15 2015 Source : BMC Res Notes. 8. URL : https://stacks.cdc.gov/view/cdc/36938 Inoguchi, Noriko et al. (2015). Structural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase: the role of tryptophan 93 in ligand orientation. 8 Inoguchi, Noriko et al. "Structural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase: the role of tryptophan 93 in ligand orientation" 8 (2015) Inoguchi, Noriko et al. "Structural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase: the role of tryptophan 93 in ligand orientation" vol. 8, 2015 Export RIS Citation Information.

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Inoguchi, Noriko ;

Chaiseeda, Kittichai

Dec 15 2015 | BMC Res Notes. 8.

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BackgroundDeoxyuridine triphosphate nucleotidohydrolase (dUTPase) hydrolyzes dUTP to dUMP and pyrophosphate to maintain the cellular thymine-uracil ra...
Influenza B Viruses with Mutation in the Neuraminidase Active Site, North Carolina, USA, 2010–11

CITE Title : Influenza B Viruses with Mutation in the Neuraminidase Active Site, North Carolina, USA, 2010–11 Personal Author(s) : Sleeman, Katrina;Sheu, Tiffany G.;Moore, Zack;Kilpatrick, Susan;Garg, Shikha;Fry, Alicia M.;Gubareva, Larisa V.; Published Date : Nov 2011 Source : Emerg Infect Dis. 17(11):2043-2046. URL : https://stacks.cdc.gov/view/cdc/23735 Sleeman, Katrina et al. (2011). Influenza B Viruses with Mutation in the Neuraminidase Active Site, North Carolina, USA, 2010–11. 17(11). Sleeman, Katrina et al. "Influenza B Viruses with Mutation in the Neuraminidase Active Site, North Carolina, USA, 2010–11" 17, no. 11 (2011) Sleeman, Katrina et al. "Influenza B Viruses with Mutation in the Neuraminidase Active Site, North Carolina, USA, 2010–11" vol. 17, no. 11, 2011 Export RIS Citation Information.

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Sleeman, Katrina ;

Sheu, Tiffany G.

Nov 2011 | Emerg Infect Dis. 17(11):2043-2046.

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Oseltamivir is 1 of 2 antiviral medications available for the treatment of influenza B virus infections. We describe and characterize a cluster of inf...
Proteomic analysis of adducted butyrylcholinesterase for biomonitoring organophosphorus exposures

CITE Title : Proteomic analysis of adducted butyrylcholinesterase for biomonitoring organophosphorus exposures Personal Author(s) : Marsillach, Judit;Hsieh, Edward J.;Richter, Rebecca J.;MacCoss, Michael J.;Furlong, Clement E.; Published Date : Nov 02 2012 Source : Chem Biol Interact. 2012; 203(1):85-90. URL : https://stacks.cdc.gov/view/cdc/52349 Marsillach, Judit et al. (2012). Proteomic analysis of adducted butyrylcholinesterase for biomonitoring organophosphorus exposures. 203(1). Marsillach, Judit et al. "Proteomic analysis of adducted butyrylcholinesterase for biomonitoring organophosphorus exposures" 203, no. 1 (2012) Marsillach, Judit et al. "Proteomic analysis of adducted butyrylcholinesterase for biomonitoring organophosphorus exposures" vol. 203, no. 1, 2012 Export RIS Citation Information.

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Marsillach, Judit ;

Hsieh, Edward J.

Nov 02 2012 | Chem Biol Interact. 2012; 203(1):85-90.

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Organophosphorus (OP) compounds include a broad group of toxic chemicals such as insecticides, chemical warfare agents and antiwear agents. The liver ...
An influenza A virus (H7N9) anti-neuraminidase monoclonal antibody with prophylactic and therapeutic activity in vivo

CITE Title : An influenza A virus (H7N9) anti-neuraminidase monoclonal antibody with prophylactic and therapeutic activity in vivo Personal Author(s) : Wilson, Jason R.;Guo, Zhu;Reber, Adrian;Kamal, Ram P.;Music, Nedzad;Gansebom, Shane;Bai, Yaohui;Levine, Min;Carney, Paul;Tzeng, Wen-Pin;Stevens, James;York, Ian A.; Published Date : 11 2016 Source : Antiviral Res. 135:48-55 URL : https://stacks.cdc.gov/view/cdc/50544 Wilson, Jason R. et al. (2016). An influenza A virus (H7N9) anti-neuraminidase monoclonal antibody with prophylactic and therapeutic activity in vivo. 135 Wilson, Jason R. et al. "An influenza A virus (H7N9) anti-neuraminidase monoclonal antibody with prophylactic and therapeutic activity in vivo" 135 (2016) Wilson, Jason R. et al. "An influenza A virus (H7N9) anti-neuraminidase monoclonal antibody with prophylactic and therapeutic activity in vivo" vol. 135, 2016 Export RIS Citation Information.

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Wilson, Jason R. ;

Guo, Zhu

11 2016 | Antiviral Res. 135:48-55

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Zoonotic A(H7N9) avian influenza viruses emerged in China in 2013 and continue to be a threat to human public health, having infected over 800 individ...
Inhibition of Mycobacterium tuberculosis PknG by non-catalytic rubredoxin domain specific modification: reaction of an electrophilic nitro-fatty acid with the Fe–S center

CITE Title : Inhibition of Mycobacterium tuberculosis PknG by non-catalytic rubredoxin domain specific modification: reaction of an electrophilic nitro-fatty acid with the Fe–S center Personal Author(s) : Gil, Magdalena;Graña, Martín;Schopfer, Francisco J.;Wagner, Tristan;Denicola, Ana;Freeman, Bruce A.;Alzari, Pedro M.;Batthyány, Carlos;Durán, Rosario; Published Date : 12 2013;12-2013; Source : Free Radic Biol Med. 2013; 65:150-161 URL : https://stacks.cdc.gov/view/cdc/41966 Gil, Magdalena et al. (2013). Inhibition of Mycobacterium tuberculosis PknG by non-catalytic rubredoxin domain specific modification: reaction of an electrophilic nitro-fatty acid with the Fe–S center. 65 Gil, Magdalena et al. "Inhibition of Mycobacterium tuberculosis PknG by non-catalytic rubredoxin domain specific modification: reaction of an electrophilic nitro-fatty acid with the Fe–S center" 65 (2013) Gil, Magdalena et al. "Inhibition of Mycobacterium tuberculosis PknG by non-catalytic rubredoxin domain specific modification: reaction of an electrophilic nitro-fatty acid with the Fe–S center" vol. 65, 2013 Export RIS Citation Information.

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Gil, Magdalena ;

Graña, Martín

12 2013 | Free Radic Biol Med. 2013; 65:150-161

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PknG from Mycobacterium tuberculosis is a Ser/Thr protein kinase that regulates key metabolic processes within the bacterial cell as well as signaling...