Review History


To increase transparency, PeerJ operates a system of 'optional signed reviews and history'. This takes two forms: (1) peer reviewers are encouraged, but not required, to provide their names (if they do so, then their profile page records the articles they have reviewed), and (2) authors are given the option of reproducing their entire peer review history alongside their published article (in which case the complete peer review process is provided, including revisions, rebuttal letters and editor decision letters).

New to public reviews? Learn more about optional signed reviews and how to write a better rebuttal letter.

Summary

  • The initial submission of this article was received on March 31st, 2014 and was peer-reviewed by 2 reviewers and the Academic Editor.
  • The Academic Editor made their initial decision on April 21st, 2014.
  • The first revision was submitted on June 9th, 2014 and was reviewed by the Academic Editor.
  • The article was Accepted by the Academic Editor on June 9th, 2014.

Version 0.2 (accepted)

· · Academic Editor

Accept

I would like to thank you very much for the efforts you made to carefully address the reviewers' comments.

Version 0.1 (original submission)

· · Academic Editor

Minor Revisions

Please address minor points raised by the reviewer #1.

Reviewer 1 ·

Basic reporting

In Fig.2, label A is missing. The samples used in Fig.2A and Fig.2B should be consistent. And the orientations of the labels for x axes in Fig.2B and Fig.2D are better to be the same.

Experimental design

No comments.

Validity of the findings

In line 437, the authors found “shNRP-1 interacts with heparin much more weakly
than Fc NRP1 (this work) or the b1-b2 domains in isolation.” The authors should state how similar the shNRP-1 is to rNRP-1, so that the property of the human truncated variant shNRP-1 differs from that of Rat fusion Fc- rNRP-1 is mainly because of the conformation or integrity of the proteins, not because of the difference of the protein sequences.

Comments for the author

It is very interesting result that the authors identified heparin binding sites of NRP-1 by selective labelling of lysines protected upon heparin binding. As the authors have mentioned, it would need further confirmation of the binding sites. Mutations of the proposed binding sites or truncation of MAM type c domain may verify the authors’ speculations in the future. And it would be nice if the authors could show the conserved protein sequence of the mapped heparin binding sites across the species.

Reviewer 2 ·

Basic reporting

No comment

Experimental design

No comment

Validity of the findings

No comment

Comments for the author

Understanding the molecular basis for Nrp’s specific binding to multiple heparin binding sites will allow us to engineer Nrp modulators that can be designed with specificity for a particular ligand. The observations made in this paper advance the search for more selective inhibitors/activators of Nrp signaling.

All text and materials provided via this peer-review history page are made available under a Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.