CIED Cybersecurity Risks in an Increasingly Connected World

Autor: Matthew B. Hazelett, Suzanne Schwartz, Jessica Paulsen

Publikováno v: Circulation. 138(12)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a762f53206cc5459e0aa3bc924e7a325
https://pubmed.ncbi.nlm.nih.gov/30354433

An overview of the security of cardiac implantable electronic devices

Autor: Linda Ricci, Seth Carmody, Suzanne Schwartz, Jessica Paulsen, Matthew B. Hazelett, Stephen Browning, Mitchell J. Shein

Publikováno v: Pacing and Clinical Electrophysiology. 40:911-912

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e68ceb33c413e0336d3c504b86d096f9
https://doi.org/10.1111/pace.13128

The structure of the first representative of Pfam family PF09836 reveals a two-domain organization and suggests involvement in transcriptional regulation

Autor: Christopher L. Rife, Kyle Ellrott, Linda Okach, Dustin C. Ernst, Prasad Burra, Dana Weekes, Edward Nigoghossian, Polat Abdubek, Gye Won Han, Silvya Oommachen, Piotr Kozbial, John Wooley, Jessica Paulsen, Henry J Tien, Slawomir K. Grzechnik, Sanjay Krishna, Amanda Nopakun, Julie Feuerhelm, Abhinav Kumar, Henry van den Bedem, Lian Duan, Mark W. Knuth, Marc C. Deller, Tamara Astakhova, Michelle Chiu, Heath E. Klock, Carol L. Farr, Hsiu-Ju Chiu, Connie Chen, Joanna C Grant, Ron Reyes, Daniel McMullan, Tiffany Wooten, Ashley M. Deacon, Nick V. Grishin, Constantina Bakolitsa, Mitchell D. Miller, Anna Grzechnik, Ian A. Wilson, Christina Puckett, Thomas Clayton, Marc André Elsliger, Andrew T. Morse, Dennis Carlton, Adam Godzik, Herbert L. Axelrod, Keith O. Hodgson, Kevin K. Jin, Scott A. Lesley, Christine B Trame, David Marciano, Hope A. Johnson, Natasha Sefcovic, Qingping Xu, Lukasz Jaroszewski, Debanu Das

Publikováno v: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10

The crystal structure of the NGO1945 gene product from N. gonorrhoeae (UniProt Q5F5IO) reveals that the N-terminal domain assigned as a domain of unknown function (DUF2063) is likely to bind DNA and that the protein may be involved in transcriptional

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b4cc1fc17c9172b8a9717ae53007ce2
https://doi.org/10.1107/s1744309109022672

The structure of KPN03535 (gi|152972051), a novel putative lipoprotein from Klebsiella pneumoniae, reveals an OB-fold

Autor: Thomas Clayton, Debanu Das, John Wooley, Marc-André Elsliger, Heath E. Klock, Polat Abdubek, Edward Nigoghossian, Marc C. Deller, Carol L. Farr, Christopher L. Rife, Sanjay Krishna, Linda Okach, Abhinav Kumar, Mark W. Knuth, Constantina Bakolitsa, Tamara Astakhova, Joanna C Grant, Adam Godzik, Kyle Ellrott, Scott A. Lesley, Qingping Xu, Hsiu-Ju Chiu, Lian Duan, Ron Reyes, Daniel McMullan, Mitchell D. Miller, Dustin C. Ernst, Dana Weekes, Anna Grzechnik, Andrew T. Morse, Gye Won Han, Julie Feuerhelm, Silvya Oommachen, Piotr Kozbial, Henry van den Bedem, Henry J Tien, Jessica Paulsen, Tiffany Wooten, Kevin K. Jin, Ashley M. Deacon, Ian A. Wilson, Christina Puckett, Keith O. Hodgson, Michelle Chiu, Amanda Nopakun, Herbert L. Axelrod, Lukasz Jaroszewski, Natasha Sefcovic, Christine B Trame, Connie Chen, David Marciano, Hope A. Johnson, Dennis Carlton

Publikováno v: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10

KPN03535 is a protein unique to K. pneumoniae. The crystal structure reveals that KPN03535 represents a novel variant of the OB-fold and is likely to be a DNA-binding lipoprotein.
KPN03535 (gi|152972051) is a putative lipoprotein of unknown func

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bd09c4d3f24cc38b69b4c4fafc18191
http://europepmc.org/articles/PMC2954213

Crystal Structure of Histidine Phosphotransfer Protein ShpA, an Essential Regulator of Stalk Biogenesis in Caulobacter crescentus

Autor: Marc C. Deller, Adam Godzik, Mark W. Knuth, Kevin K. Jin, Joanna C Grant, Ron Reyes, Ylva Elias, Henry van den Bedem, Andrew T. Morse, Linda Okach, Mitchell D. Miller, Anna Grzechnik, Keith O. Hodgson, Christopher L. Rife, Hsiu-Ju Chiu, Piotr Kozbial, Prasad Burra, Lian Duan, Heath E. Klock, Tamara Astakhova, Julie Feuerhelm, Jessica Paulsen, Abhinav Kumar, Thomas Clayton, Marc André Elsliger, Dana Weekes, Christina V. Trout, Gye Won Han, Edward Nigoghossian, Silvya Oommachen, Daniel McMullan, John Wooley, Polat Abdubek, Sanjay Krishna, Dennis Carlton, Natasha Sefcovic, Lukasz Jaroszewski, Qingping Xu, Christine B Trame, David Marciano, Ian A. Wilson, Scott A. Lesley, Ashley M. Deacon, Slawomir K. Grzechnik

Publikováno v: Journal of Molecular Biology. 390:686-698

Cell cycle regulated stalk biogenesis in Caulobacter crescentus is controlled by a multi-step phosphorelay system consisting of the hybrid histidine kinase ShkA, the histidine-phosphotransfer protein ShpA and the response regulator TacA. ShpA shuttle

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::adfb220b9e3c874a22e174ef0321e280
https://doi.org/10.1016/j.jmb.2009.05.023