Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Bradley P, Klemm"'
Autor:
Jonathan Bouvette, Hsuan-Fu Liu, Xiaochen Du, Ye Zhou, Andrew P. Sikkema, Juliana da Fonseca Rezende e Mello, Bradley P. Klemm, Rick Huang, Roel M. Schaaper, Mario J. Borgnia, Alberto Bartesaghi
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
Tomographic reconstructions of cryopreserved specimens enable in-situ structural studies. Here, the authors present the beam image-shift electron cryo-tomography (BISECT) approach that accelerates data collection speed and improves the map resolution
Externí odkaz:
https://doaj.org/article/984e7bb3da884354b7ff3bc7cde40146
Autor:
Bradley P, Klemm, Deepa, Singh, Cassandra E, Smith, Allen L, Hsu, Lucas B, Dillard, Juno M, Krahn, Robert E, London, Geoffrey A, Mueller, Mario J, Borgnia, Roel M, Schaaper
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(37)
Levels of the cellular dNTPs, the direct precursors for DNA synthesis, are important for DNA replication fidelity, cell cycle control, and resistance against viruses.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6f8f7ec4e6a8fb59038bd37189953473
https://pubmed.ncbi.nlm.nih.gov/36067314
https://pubmed.ncbi.nlm.nih.gov/36067314
Autor:
Bradley P. Klemm, Deepa Singh, Cassandra E. Smith, Allen L. Hsu, Lucas B. Dillard, Juno M. Krahn, Robert E. London, Geoffrey A. Mueller, Mario J. Borgnia, Roel M. Schaaper
Publikováno v:
Proceedings of the National Academy of Sciences. 119
Levels of the cellular dNTPs, the direct precursors for DNA synthesis, are important for DNA replication fidelity, cell cycle control, and resistance against viruses. Escherichia coli encodes a dGTPase (2′-deoxyguanosine-5′-triphosphate [dGTP] tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9a4e42da2ab3f1e7ea98051372b7c643
https://doi.org/10.1073/pnas.2123092119
https://doi.org/10.1073/pnas.2123092119
Autor:
Bradley P. Klemm, Andrew P. Sikkema, Allen L. Hsu, James C. Horng, Traci M. Tanaka Hall, Mario J. Borgnia, Roel M. Schaaper
Publikováno v:
The Journal of biological chemistry. 298(7)
Deoxynucleoside triphosphate (dNTP) triphosphohydrolases (dNTPases) are important enzymes that may perform multiple functions in the cell, including regulating the dNTP pools and contributing to innate immunity against viruses. Among the homologs tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c69410ea22f7531287e479571a17d7c4
https://pubmed.ncbi.nlm.nih.gov/35643313
https://pubmed.ncbi.nlm.nih.gov/35643313
Autor:
Hsuan-Fu Liu, Bradley P. Klemm, Roel M. Schaaper, Xiaochen Du, Mario J. Borgnia, Ye Zhou, Rick Huang, Andrew P. Sikkema, Jonathan Bouvette, Juliana da Fonseca Rezende e Mello, Alberto Bartesaghi
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
Tomographic reconstruction of cryopreserved specimens imaged in an electron microscope followed by extraction and averaging of sub-volumes has been successfully used to derive atomic models of macromolecules in their biological environment. Eliminati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8204ad924443f22732a4c163039b4989
http://europepmc.org/articles/PMC8009872
http://europepmc.org/articles/PMC8009872
Autor:
Bradley P. Klemm, Nancy Wu, Yu Chen, Xin Liu, Kipchumba J. Kaitany, Michael J. Howard, Carol A. Fierke
Publikováno v:
Biomolecules, Vol 6, Iss 2, p 27 (2016)
Ribonuclease P (RNase P) is an essential endonuclease responsible for catalyzing 5’ end maturation in precursor transfer RNAs. Since its discovery in the 1970s, RNase P enzymes have been identified and studied throughout the three domains of life.
Externí odkaz:
https://doaj.org/article/e2ae747c1db8455881486b85482053b5
Autor:
Aranganathan Shanmuganathan, Adam Z. Thelen, Carol A. Fierke, Agnes Karasik, Kipchumba J. Kaitany, Nathaniel D. Jackson, Matthew J. Henley, Bradley P. Klemm, Markos Koutmos, Allison J.L. Dewar
Publikováno v:
RNA. 23:1860-1873
Protein-only ribonuclease P (PRORP) is an enzyme responsible for catalyzing the 5′ end maturation of precursor transfer ribonucleic acids (pre-tRNAs) encoded by various cellular compartments in many eukaryotes. PRORPs from plants act as single-subu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5434c01274c8dc161b16c1d286abbe5c
https://doi.org/10.1261/rna.061457.117
https://doi.org/10.1261/rna.061457.117
Autor:
Nancy Wu, Carol A. Fierke, Wan Hsin Lim, Bradley P. Klemm, Aranganathan Shanmuganathan, Xin Liu, Michael J. Howard, Markos Koutmos
A first step in processing mitochondrial precursor tRNA (pre-tRNA) is cleavage of the 5’ leader catalyzed by ribonuclease P (RNase P). Human mitochondrial RNase P (mtRNase P) is composed of three protein subunits: mitochondrial RNase P protein (MRP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7abe0b82c35b66704a7965dde4c0e3b1
Autor:
Michael J. Howard, Christine Mei, Aranganathan Shanmuganathan, Bradley P. Klemm, Carol A. Fierke, Markos Koutmos, Agnes Karasik
Publikováno v:
RNA. 22:782-792
Ribonuclease P (RNase P) catalyzes the cleavage of leader sequences from precursor tRNA (pre-tRNA). Typically, these enzymes are ribonucleic protein complexes that are found in all domains of life. However, a new class of RNase P has been discovered
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2d6506a3b6e6ebe69136132d1346e81
https://doi.org/10.1261/rna.055541.115
https://doi.org/10.1261/rna.055541.115
Publikováno v:
Journal of Biological Chemistry. 290:13454-13464
Ribonuclease P (RNase P) is an endonuclease that catalyzes the essential removal of the 5′ end of tRNA precursors. Until recently, all identified RNase P enzymes were a ribonucleoprotein with a conserved catalytic RNA component. However, the discov
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6de4ac26ac600dd746768765c1832611
https://doi.org/10.1074/jbc.m115.644831
https://doi.org/10.1074/jbc.m115.644831