D
Dmitry Temiakov
Researcher at Thomas Jefferson University
Publications - 44
Citations - 2702
Dmitry Temiakov is an academic researcher from Thomas Jefferson University. The author has contributed to research in topics: Transcription (biology) & Polymerase. The author has an hindex of 24, co-authored 38 publications receiving 2275 citations. Previous affiliations of Dmitry Temiakov include Rowan University & Oregon Health & Science University.
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Journal ArticleDOI
Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease
Bin Lu,Jae Lee,Xiaobo Nie,Min Li,Yaroslav I. Morozov,Sundararajan Venkatesh,Daniel F. Bogenhagen,Dmitry Temiakov,Carolyn K. Suzuki +8 more
TL;DR: It is demonstrated that TFAM is phosphorylated within its HMG box 1 (HMG1) by cAMP-dependent protein kinase in mitochondria, which provides mechanisms for rapid fine-tuning of TFAM function and abundance in mitochondaria, which are crucial for maintaining and expressing mtDNA.
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Mitochondrial replacement in human oocytes carrying pathogenic mitochondrial DNA mutations
Eunju Kang,Eunju Kang,Jun Wu,Nuria Marti Gutierrez,Amy Koski,Rebecca Tippner-Hedges,Karen Agaronyan,Aida Platero-Luengo,Paloma Martinez-Redondo,Hong Ma,Hong Ma,Yeon-Mi Lee,Tomonari Hayama,Crystal Van Dyken,Xinjian Wang,Shiyu Luo,Riffat Ahmed,Ying Li,Dongmei Ji,Dongmei Ji,Refik Kayali,Cengiz Cinnioglu,Susan B. Olson,Jeffrey T. Jensen,David Battaglia,David M. Lee,Diana Wu,Taosheng Huang,Don P. Wolf,Dmitry Temiakov,Juan Carlos Izpisua Belmonte,Paula Amato,Shoukhrat Mitalipov +32 more
TL;DR: A polymorphism within the conserved sequence box II region of the D-loop is identified as a plausible cause of preferential replication of specific mtDNA haplotypes, and a matching paradigm for selecting compatible donor mtDNA for MRT is proposed.
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Structure of a T7 RNA Polymerase Elongation Complex at 2.9 A Resolution
Tahir H. Tahirov,Dmitry Temiakov,Michael Anikin,Vsevolod Patlan,William T. McAllister,Dmitry G. Vassylyev,Shigeyuki Yokoyama +6 more
TL;DR: The crystal structure of a T7 RNA polymerase elongation complex shows that incorporation of an 8-base-pair RNA–DNA hybrid into the active site of the enzyme induces a marked rearrangement of the amino-terminal domain, resulting in a structure that provides elements required for stable transcription elongation.
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Human Mitochondrial Transcription Revisited ONLY TFAM AND TFB2M ARE REQUIRED FOR TRANSCRIPTION OF THE MITOCHONDRIAL GENES IN VITRO
Dmitry Litonin,Marina Sologub,Yonghong Shi,Maria Savkina,Michael Anikin,Maria Falkenberg,Claes M. Gustafsson,Dmitry Temiakov +7 more
TL;DR: In this paper, the authors found that TFAM and TFB2M act synergistically and increase transcription efficiency 100-200fold as compared with RNA polymerase alone, and that only two essential initiation factors are required to drive transcription of the mitochondrial genome.
Journal ArticleDOI
Structural Basis for Substrate Selection by T7 RNA Polymerase
Dmitry Temiakov,Vsevolod Patlan,Michael Anikin,William T. McAllister,Shigeyuki Yokoyama,Dmitry G. Vassylyev +5 more
TL;DR: The structure of T7 RNAP elongation complex suggests a novel mechanism, in which the substrate selection occurs prior to the isomerization to the catalytically active conformation, which might be universal for all RNAPs.