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Review
Peer-Review Record

3D Structure and Function of Glycosyltransferases Involved in N-glycan Maturation

Int. J. Mol. Sci. 2020, 21(2), 437; https://doi.org/10.3390/ijms21020437
by Masamichi Nagae 1,*, Yoshiki Yamaguchi 2, Naoyuki Taniguchi 3 and Yasuhiko Kizuka 4,*
Reviewer 1: Anonymous
Reviewer 2: Anonymous
Reviewer 3: Anonymous
Int. J. Mol. Sci. 2020, 21(2), 437; https://doi.org/10.3390/ijms21020437
Submission received: 17 December 2019 / Revised: 6 January 2020 / Accepted: 8 January 2020 / Published: 9 January 2020

Round 1

Reviewer 1 Report

Excellent review by Nagae et al describing the status of the structure biology of glycosyltransferases. I have four minor comments/recommendations that could improve an already very good review.

1. Section 2 needs a title.

2. Figure legends wold benefit from a better description of what is seen in the figure.

3. Figures are not friendly for color-blinded researchers. Changing the figures would preferable, but at least is necessary to change the colors of the arrows (for example figure 2a).

4. The review would greatly benefit form one figure (or more) describing the catalytic mechanism of key enzymes.

Author Response

Reviewer 1

Excellent review by Nagae et al describing the status of the structure biology of glycosyltransferases. I have four minor comments/recommendations that could improve an already very good review.

 

Section 2 needs a title.

Response:

We added a title, “Structure and function of glycosyltransferases for N-glycan branching”.

 

Figure legends would benefit from a better description of what is seen in the figure.

Response:

According to the reviewer’s suggestion, we added and modified several sentences in the Figure legends.

 

Figures are not friendly for color-blinded researchers. Changing the figures would preferable, but at least is necessary to change the colors of the arrows (for example figure 2a).

Response:

Thank you very much for pointing it out. We have changed the color of arrows in figures (Figure 2a, 3a, 4a and 5a). In addition, the residue numbers of Figure 3e are replaced to underline.

 

The review would greatly benefit form one figure (or more) describing the catalytic mechanism of key enzymes.

Response:

We understand that such figure could be useful, but unfortunately the catalytic mechanisms of not all enzymes have been clarified, and it would take more time to complete such figures.

 

Reviewer 2 Report

English has to be checked.

This review is a really impressive work and the only thing I can complain about its english. But after minor spell check I think it has to be accepted. It is original and novel enough to publish.

Author Response

Reviewer 2

English has to be checked.

This review is a really impressive work and the only thing I can complain about its english. But after minor spell check I think it has to be accepted. It is original and novel enough to publish.

Response:

Thank you very much for your positive comments. We apologize for our poor English. We have read through the paper again and checked our English. We hope the revised paper is now acceptable.

 

Reviewer 3 Report

This is a well written, comprehensive review article. My only suggestion is that, for the sake of completeness, the authors briefly include some basic information about O-glycosylation.

Author Response

Reviewer 3

This is a well written, comprehensive review article. My only suggestion is that, for the sake of completeness, the authors briefly include some basic information about O-glycosylation.

 

Response

Thank you very much for your positive comments. We have added the following sentences in Introduction, “In mammalian cells, another major type of glycan, O-glycan, is also attached to Ser/Thr residues and regulates various protein functions. This type of glycan is also biosynthesized by the concerted actions of glycosyltransferases in the Golgi and involved in many physiological and pathological phenomena as reviewed by several papers [1,4].”

 

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