Skip To Main Content
William D. Barshop on Muck Rack

William D. Barshop

As seen in: ACS Publications, BioRxiv, Cell Press, The Planet Weekly
Is this you? As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work. Claim your profile

Get in touch with William D.

Contact William D., search articles and posts on X, monitor coverage, and track replies from one place.

Learn more about Muck Rack

Actions

Share this page

Is this you?

As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work.
Claim your profile

Articles

Autonomous Dissociation-type Selection for Glycoproteomics Using a Real-Time Library Search

|
By Emmajay Sutherland, Tim Veth, William D. Barshop, Jacob Russell
| dx.doi.org
Wednesday, November 13, 2024 Please be aware that pubs.acs.org is undergoing maintenance on Friday, September 6, at 6 p.m. EDT that may have an impact on your experience. During this time, you may not be able to access certain features like login, purchasing single articles, saving searches or running existing saved searches, modifying your e-Alert preferences, or accessing Librarian administrative functions. We appreciate your patience as we continue to improve the ACS Publications platform.
Open in Who Shared Issue with article?

Autonomous Dissociation-type Selection for Glycoproteomics Using a Real-Time Library Search

|
By Emmajay Sutherland, Tim Veth, William D. Barshop, Jacob Russell
| ACS Publications
Introduction Click to copy section linkSection link copied! Protein glycosylation is a highly heterogeneous collection of co- and post-translational modifications.
Open in Who Shared Issue with article?

Function and interactions of a protein bridge between the inner membrane complex and subpellicular microtubules in Toxoplasma gondii

|
By Emily Cheng, Andy S. Moon, William D. Barshop, James A. Wohlschlegel
| BioRxiv
Abstract Toxoplasma gondii is an obligate intracellular parasite that utilizes peripheral membrane and cytoskeletal structures for critical functions such as host cell invasion, replication, and maintaining cellular morphology. These structures include the inner membrane complex (IMC) as well as the underlying longitudinal subpellicular microtubules (SPMTs) that provide support for the IMC and give the parasite its distinctive crescent shape.
Open in Who Shared Issue with article?
See all 18 articles