278
Views
4
CrossRef citations to date
0
Altmetric
Research Articles

Predicting interfacial hot-spot residues that stabilize protein-protein interfaces in oligomeric membrane-toxin pores through hydrogen bonds and salt bridges

ORCID Icon, &
Pages 20-34 | Received 04 Aug 2019, Accepted 28 Nov 2019, Published online: 29 Jan 2020

Keep up to date with the latest research on this topic with citation updates for this article.

Read on this site (1)

Youngki You & Joydip Das. (2022) Molecular dynamics simulation studies on binding of activator and inhibitor to Munc13-1 C1 in the presence of membrane. Journal of Biomolecular Structure and Dynamics 40:24, pages 14160-14175.
Read now

Articles from other publishers (3)

Avijeet Kulshrestha, Satyaghosh Maurya, Twinkle Gupta, Rahul Roy, Sudeep N Punnathanam & K. Ganapathy Ayappa. (2022) Conformational Flexibility Is a Key Determinant for the Lytic Activity of the Pore-Forming Protein, Cytolysin A. The Journal of Physical Chemistry B 127:1, pages 69-84.
Crossref
Subhadip Basu, Biswajit Gorai, Bikramjit Basu & Prabal K. Maiti. (2021) Electric Field-Mediated Fibronectin–Hydroxyapatite Interaction: A Molecular Insight. The Journal of Physical Chemistry B 125:1, pages 3-16.
Crossref
Rajat Desikan, Amit Behera, Prabal K. Maiti & K. Ganapathy Ayappa. 2021. Pore-Forming Toxins. Pore-Forming Toxins 461 502 .

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.