Results 161 to 170 of about 4,851 (193)
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ClpX/P-Dependent Degradation of Novel Substrates in Streptococcus mutans
Journal of Bacteriology, 2022ClpX/P is a major intracellular proteolytic complex that is responsible for protein quality control in the cell. ClpX, an AAA+ ATPase, distinguishes the potential substrates by recognizing short motifs at the C-terminal end of proteins and delivers the substrates for degradation by ClpP protease.
Vivek Gurung, Indranil Biswas
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Protein homeostasis is essential for cyanobacteria to maintain proper cellular function under adverse and fluctuating conditions. The AAA+ superfamily of proteolytic complexes in cyanobacteria plays a critical role in this process, including ClpXP, which
Fangfang Cai, Xin Liu, Feng Ge
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Maintenance of mitochondrial genome distribution by mitochondrial AAA+ protein ClpX
Experimental Cell Research, 2012The segregation of mitochondrial DNA (mtDNA) is important for the maintenance and transmission of the genome between generations. Recently, we clarified that human mitochondrial transcription factor A (TFAM) is required for equal distribution and symmetric segregation of mtDNA in cultured cells; however, the molecular mechanism involved is largely ...
Katsumi, Kasashima +2 more
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Comparison with CLPX II airborne data using DMRT model
2009 IEEE International Geoscience and Remote Sensing Symposium, 2009In this paper, we considered a physical-based model which use numerical solution of Maxwell Equations in three-dimensional simulations and apply into Dense Media Radiative Theory (DMRT). The model is validated in two specific dataset from the second Cold Land Processes Experiment (CLPX II) at Alaska and Colorado. The data were all obtain by the Ku-band
Xiaolan Xu +4 more
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Communication between ClpX and ClpP during substrate processing and degradation
Nature Structural & Molecular Biology, 2004In the ClpXP compartmental protease, ring hexamers of the AAA(+) ClpX ATPase bind, denature and then translocate protein substrates into the degradation chamber of the double-ring ClpP(14) peptidase. A key question is the extent to which functional communication between ClpX and ClpP occurs and is regulated during substrate processing.
Shilpa A, Joshi +3 more
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The Impact of Snow Model Complexity at Three CLPX Sites
Journal of Hydrometeorology, 2008Abstract Many studies have developed snow process understanding by exploring the impact of snow model complexity on simulation performance. This paper revisits this topic using several recently developed land surface models, including the Simplified Simple Biosphere Model (SSiB); Noah; Variable Infiltration Capacity (VIC); Community Land
Xia Feng +5 more
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Regulation of Erythroid Heme Synthesis By the Mitochondrial Clpx Unfoldase
Blood, 2019Differentiating erythroid cells synthesize large quantities of heme for hemoglobinization. While the transcriptional regulation and enzymatic mechanisms of the heme synthetic enzymes are well characterized, we lack mechanistic understanding of how their protein stability, cofactor incorporation and functional interactions with mitochondrial ...
Yvette Y Yien +6 more
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[Bacterial ClpX protease structure and function--a review].
Wei sheng wu xue bao = Acta microbiologica Sinica, 2011ClpX is a member of Hsp100 (heat-shock protein) family which is conserved among organisms. Hsp100/ Clp implicates in stress resistance, intracellular protein turn-over, DNA replication and regulation of gene expression. Tuberculosis remains one of the major threats to human health.
Lin, Wang, Jianping, Xie
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Funkce šaperonu ClpX u bakterií
2020Intracellular proteolysis is an essential regulatory process that affects cellular physiology. Since proteolysis destroys proteins irreversibly, this process must be strictly controlled. The AAA+ proteins are the key factors in regulated proteolysis in bacteria.
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Mutations in genes involved in the heme biosynthesis pathway can cause various hematologic disorders. Previous research determined that heme synthesis is regulated by the mitochondrial AAA+ unfoldase ClpX through the activation of ALAS which initiates the first step of the pathway. A reported dominant mutation in the ATPase active site of human ClpX, p.
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