D
Dmitry G. Vassylyev
Researcher at University of Alabama at Birmingham
Publications - 90
Citations - 8700
Dmitry G. Vassylyev is an academic researcher from University of Alabama at Birmingham. The author has contributed to research in topics: RNA polymerase & Thermus thermophilus. The author has an hindex of 46, co-authored 89 publications receiving 8270 citations. Previous affiliations of Dmitry G. Vassylyev include Panasonic & University of Alabama.
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Journal ArticleDOI
Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution
Dmitry G. Vassylyev,Shun-ichi Sekine,Oleg Laptenko,Jookyung Lee,Marina N. Vassylyeva,Sergei Borukhov,Shigeyuki Yokoyama +6 more
TL;DR: The crystal structure of a bacterial RNA polymerase holoenzyme from Thermus thermophilus at 2.6 Å resolution provides insight into the structural organization of transcription intermediate complexes and into the mechanism of transcription initiation.
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Surface of bacteriorhodopsin revealed by high-resolution electron crystallography
Yoshiaki Kimura,Dmitry G. Vassylyev,Dmitry G. Vassylyev,Atsuo Miyazawa,Atsuo Miyazawa,Akinori Kidera,Masaaki Matsushima,Kaoru Mitsuoka,Kazuyoshi Murata,Teruhisa Hirai,Yoshinori Fujiyoshi,Yoshinori Fujiyoshi +11 more
TL;DR: In this paper, electron microscopy was used to obtain images of bacteriorhodopsin at 3.0 A resolution, revealing the distribution of charged residues on both sides of the membrane surface.
Journal ArticleDOI
Structural basis for transcription elongation by bacterial RNA polymerase
Dmitry G. Vassylyev,Marina N. Vassylyeva,Anna Perederina,Tahir H. Tahirov,Irina Artsimovitch +4 more
TL;DR: The 2.5-Å resolution structure of the Thermus thermophilus EC is reported; the structure reveals the post-translocated intermediate with the DNA template in the active site available for pairing with the substrate.
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Regulation through the Secondary Channel—Structural Framework for ppGpp-DksA Synergism during Transcription
Anna Perederina,Vladimir Svetlov,Marina N. Vassylyeva,Tahir H. Tahirov,Shigeyuki Yokoyama,Irina Artsimovitch,Dmitry G. Vassylyev +6 more
TL;DR: Biochemical analysis demonstrates that DksA affects transcript elongation, albeit differently from GreA; augments ppGpp effects on initiation; and binds directly to RNAP, positioning the Asp residues near the active site.
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Structural basis for substrate loading in bacterial RNA polymerase
Dmitry G. Vassylyev,Marina N. Vassylyeva,Jinwei Zhang,Murali Palangat,Irina Artsimovitch,Robert Landick +5 more
TL;DR: The 30-A resolution structures of the Thermus thermophilus elongation complex (EC) with a non-hydrolysable substrate analogue, adenosine-5′-[(α,β)-methyleno]-triphosphate (AMPcPP), and with AMPcPP plus the inhibitor streptolydigin were reported in this paper.