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Volume 23
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Correction to Int. J. Mol. Sci. 2021, 22(15), 7779.
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Correction

Correction: Chaudhuri et al. Diverse Functions of Tim50, a Component of the Mitochondrial Inner Membrane Protein Translocase. Int. J. Mol. Sci. 2021, 22, 7779

by
Minu Chaudhuri
*,
Anuj Tripathi
and
Fidel Soto Gonzalez
Department of Microbiology, Immunology, and Physiology, Meharry Medical College, Nashville, TN 37208, USA
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2022, 23(14), 7496; https://doi.org/10.3390/ijms23147496
Submission received: 21 January 2022 / Accepted: 27 January 2022 / Published: 6 July 2022
(This article belongs to the Special Issue Research of Mitochondrial Function, Structure, Dynamics and Intracellular Organization)
Browse Figure
Versions Notes
The authors wish to make the following correction to this paper [1]:
Changes in Figure 5, because Figure 5B misprinted as a duplication of Figure 5A by authors mistakenly during the proofreading. The correct Figure 5 is shown below. Figure changes will not affect the description and conclusion of the manuscript.
The authors would like to apologize for any inconvenience caused to the readers by these changes. This correction was approved by the Academic Editor. The original publication has also been updated.

Reference

  1. Chaudhuri, M.; Tripathi, A.; Gonzalez, F.S. Diverse Functions of Tim50, a Component of the Mitochondrial Inner Membrane Protein Translocase. Int. J. Mol. Sci. 2021, 22, 7779. [Google Scholar] [CrossRef] [PubMed]
Ijms 23 07496 g005 550
Figure 5. Primary sequence alignment of ScTim50 with hTim50 (A) and TbTim50 (B). Relatively conserved regions are shown. Identical AA residues are indicated. The conserved and non-conserved cysteine residues are indicated by blue ^ and underscore, respectively. Leucine residues within the conserved coiled-coil region (L279, L282, and L286 in ScTim50) are marked by ⧮. AA residues R214 and K217 located on the lateral side of the β-hairpin loop that are responsible for interaction with Tim23 are indicated by *. Three AA pairs that are important for the interaction between ScTim50 and ScTim23 are shown by asterisks of different colors (*, *, and *).
Figure 5. Primary sequence alignment of ScTim50 with hTim50 (A) and TbTim50 (B). Relatively conserved regions are shown. Identical AA residues are indicated. The conserved and non-conserved cysteine residues are indicated by blue ^ and underscore, respectively. Leucine residues within the conserved coiled-coil region (L279, L282, and L286 in ScTim50) are marked by ⧮. AA residues R214 and K217 located on the lateral side of the β-hairpin loop that are responsible for interaction with Tim23 are indicated by *. Three AA pairs that are important for the interaction between ScTim50 and ScTim23 are shown by asterisks of different colors (*, *, and *).
Ijms 23 07496 g005
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MDPI and ACS Style

Chaudhuri, M.; Tripathi, A.; Gonzalez, F.S. Correction: Chaudhuri et al. Diverse Functions of Tim50, a Component of the Mitochondrial Inner Membrane Protein Translocase. Int. J. Mol. Sci. 2021, 22, 7779. Int. J. Mol. Sci. 2022, 23, 7496. https://doi.org/10.3390/ijms23147496

AMA Style

Chaudhuri M, Tripathi A, Gonzalez FS. Correction: Chaudhuri et al. Diverse Functions of Tim50, a Component of the Mitochondrial Inner Membrane Protein Translocase. Int. J. Mol. Sci. 2021, 22, 7779. International Journal of Molecular Sciences. 2022; 23(14):7496. https://doi.org/10.3390/ijms23147496

Chicago/Turabian Style

Chaudhuri, Minu, Anuj Tripathi, and Fidel Soto Gonzalez. 2022. "Correction: Chaudhuri et al. Diverse Functions of Tim50, a Component of the Mitochondrial Inner Membrane Protein Translocase. Int. J. Mol. Sci. 2021, 22, 7779" International Journal of Molecular Sciences 23, no. 14: 7496. https://doi.org/10.3390/ijms23147496

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