J
Jaru Jancarik
Researcher at University of California, Berkeley
Publications - 28
Citations - 4718
Jaru Jancarik is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: Thermotoga maritima & Protein structure. The author has an hindex of 20, co-authored 28 publications receiving 4651 citations. Previous affiliations of Jaru Jancarik include Lawrence Berkeley National Laboratory.
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Crystal structure of YjeQ from Thermotoga maritima contains a circularly permuted GTPase domain
TL;DR: The overall structural features of TmYjeQ make it a good candidate for an RNA-binding protein, which is consistent with the biochemical data of the YjeQ subfamily in binding to the ribosome.
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Crystal structure of a phosphatase with a unique substrate binding domain from Thermotoga maritima
Dong Hae Shin,Anne Roberts,Jaru Jancarik,Hisao Yokota,Rosalind Kim,David E. Wemmer,David E. Wemmer,Sung-Hou Kim,Sung-Hou Kim +8 more
TL;DR: The superposition of active site residues with other HAD family members indicates that TM0651 is very likely a phosphatase that acts through the formation of a phosphoaspartate intermediate, which is supported by both NMR titration data and a biochemical assay.
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Crystal structure of NusA from Thermotoga Maritima and functional implication of the N-Terminal Domain
Dong Hae Shin,Henry Huy Nguyen,Henry Huy Nguyen,Jaru Jancarik,Hisao Yokota,Rosalind Kim,Sung-Hou Kim,Sung-Hou Kim +7 more
TL;DR: Structural comparison between TmNusA and Mycobacterium tuberculosis NusA reveals a possible hinge motion between NTD and RBD, and a functional implication of the NTD in its interaction with RNA polymerase is discussed.
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Crystal Structure of the “PhoU-Like” Phosphate Uptake Regulator from Aquifex aeolicus
Vaheh Oganesyan,Natalia Oganesyan,Paul D. Adams,Jaru Jancarik,Hisao Yokota,Rosalind Kim,Sung-Hou Kim,Sung-Hou Kim +7 more
TL;DR: It is proposed that gene regulation by PhoU may occur by association of PHOU_AQUAE with the ATPase domain of the histidine kinase PhoR, promoting release of its substrate PhoB.
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Structure of OsmC from Escherichia coli: a salt-shock-induced protein.
Dong Hae Shin,In Geol Choi,Didier Busso,Jaru Jancarik,Hisao Yokota,Rosalind Kim,Sung-Hou Kim,Sung-Hou Kim +7 more
TL;DR: A detailed analysis of structures and sequence comparisons in the OsmC sequence family revealed that each subfamily has unique motifs, suggesting that the OSMC sequenceFamily has a peroxiredoxin function and has a unique structure compared with other peroxIREDoxin families.