2019
DOI: 10.1016/j.tice.2018.08.009
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Cryo-electron tomography for the structural study of mitochondrial translation

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Cited by 9 publications
(6 citation statements)
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“…[34][35][36] The dynamics can be seen in sub-nanometer resolution with cryoelectron tomography. 32,33 There may be unique orientations and distribution in different types of cells, and a close association with microtubules in some regions. 37,38 In sites where the energy requirements are relatively high, mitochondria may appear more static and provide ATP directly on-site.…”
Section: Mitochondrial Ultrastructurementioning
confidence: 99%
See 1 more Smart Citation
“…[34][35][36] The dynamics can be seen in sub-nanometer resolution with cryoelectron tomography. 32,33 There may be unique orientations and distribution in different types of cells, and a close association with microtubules in some regions. 37,38 In sites where the energy requirements are relatively high, mitochondria may appear more static and provide ATP directly on-site.…”
Section: Mitochondrial Ultrastructurementioning
confidence: 99%
“…1C ) with active division and fusion. 32 , 33 The mitochondrial content and morphology are altered by cellular stress. In living cells, the net mitochondrial content or the mitochondrial mass depends on the balance between mitochondrial biogenesis and degradation.…”
Section: Introductionmentioning
confidence: 99%
“…This technique is versatile, allowing for the examination of a wide array of macromolecular complexes in vitro [7] and in situ [8], including amyloid filaments [9][10][11][12][13][14] and enveloped viruses such as SARS-CoV-2 [15]. CryoET can also probe the structure of other clinically-relevant samples ranging from individual organelles [16,17] and cells [18,19] to complex tissue sections [20][21][22][23][24]. Insights from cryoET data analysis can facilitate understanding dynamic molecular processes such as viral infections [25][26][27][28][29][30], enable pathology diagnosis [31,32], and reveal the impacts of potential therapeutic interventions [19], among other biomedical applications.…”
Section: Introductionmentioning
confidence: 99%
“…Cryoelectron tomography (cryoET) has obvious relevance for such a task [15]. However, since we basically have only single specimens in cryoET (setting aside the method of subtomogram averaging [15] that still requires many identical molecules), we cannot perform averaging to improve signal-to-noise ratio (SNR) and the resolution remains to be ≈ 3 − 5 nm [16]. This value falls just short of about ≈ 2 − 3 nm that is needed for identification of protein molecules in the tomogram [17].…”
Section: Introductionmentioning
confidence: 99%