T
Thomas C. Squier
Researcher at Western University of Health Sciences
Publications - 83
Citations - 3336
Thomas C. Squier is an academic researcher from Western University of Health Sciences. The author has contributed to research in topics: Calmodulin & Phospholamban. The author has an hindex of 27, co-authored 83 publications receiving 3128 citations. Previous affiliations of Thomas C. Squier include Edward Via College of Osteopathic Medicine & Pacific Northwest National Laboratory.
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Journal ArticleDOI
Respiration of metal (hydr)oxides by shewanella and geobacter: a key role for multihaem c-type cytochromes
TL;DR: Multihaem c‐Cyts play critical roles in S. oneidensis MR‐1‐ and G.’sulfurreducens‐mediated dissimilatory reduction of solid metal (hydr)oxides by facilitating ET across the bacterial cell envelope.
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Isolation of a high-affinity functional protein complex between OmcA and MtrC: Two outer membrane decaheme c-type cytochromes of Shewanella oneidensis MR-1.
Liang Shi,Baowei Chen,Zheming Wang,Dwayne A. Elias,M. Uljana Mayer,Yuri A. Gorby,Shuison Ni,Brian H. Lower,David W. Kennedy,David S. Wunschel,Heather M. Mottaz,Matthew J. Marshall,Eric A. Hill,Alexander S. Beliaev,John M. Zachara,James K. Fredrickson,Thomas C. Squier +16 more
TL;DR: It is demonstrated that OmcA and MtrC can interact directly with each other to form a stable complex that is consistent with their role in the electron transport pathway of S. oneidensis MR-1.
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High-affinity binding and direct electron transfer to solid metals by the Shewanella oneidensis MR-1 outer membrane c-type cytochrome OmcA.
Yijia Xiong,Liang Shi,Baowei Chen,M. Uljana Mayer,Brian H. Lower,Yuri Londer,Saumyaditya Bose,Michael F. Hochella,James K. Fredrickson,Thomas C. Squier +9 more
TL;DR: Binding is highly favorable, with a partition coefficient of approximately 2 x 105 (DeltaGo' = -28 kJ/mol), where approximately 1014 OmcA proteins bind per cm2 to the solid metal surface, indicating the utility of using purified OmcC in the construction of a biofuel cell.
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Redox modulation of cellular signaling and metabolism through reversible oxidation of methionine sensors in calcium regulatory proteins.
TL;DR: It is suggested that under acute conditions, such as inflammation or ischemia, these types of mechanisms ensure minimal nonspecific cellular damage, allowing for rapid restoration of cellular function through repair of oxidized methionines by methionine sulfoxide reductases and degradation pathways after restoration of normal cellular redox conditions.
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Proteomic analysis of Salmonella enterica serovar typhimurium isolated from RAW 264.7 macrophages: identification of a novel protein that contributes to the replication of serovar typhimurium inside macrophages.
Liang Shi,Joshua N. Adkins,James R. Coleman,Athena A. Schepmoes,Alice Dohnkova,Heather M. Mottaz,Angela D. Norbeck,Samuel O. Purvine,Nathan P. Manes,Heather S. Smallwood,Haixing Wang,John Forbes,Philippe Gros,Sergio Uzzau,Karin D. Rodland,Fred Heffron,Richard D. Smith,Thomas C. Squier +17 more
TL;DR: Deletion of the gene encoding STM3117 resulted in a dramatic reduction in the ability of STM to colonize wild-type RAW 264.7 macrophages, demonstrating a critical involvement of STm3117 in promoting the replication of ST M inside macrophage infection.