Skip To Main Content
Teruhiko Matsubara on Muck Rack

Teruhiko Matsubara

As seen in: Wiley Online Library, Royal Society of Chemistry, The Journal of Biological Chemistry
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 Teruhiko

Contact Teruhiko, 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

Effects of the Magnetic Orientation of M13 Bacteriophage on Phage Display Selection

|
By Shuxu Wang, Noriyuki Uchida, Teruhiko Matsubara, Kento Ueno
| Wiley Online Library Verified
Supporting Information As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors.
Open in Who Shared View Duplicates (700) Issue with article?

Peptide mimotopes to emulate carbohydrates

|
By Teruhiko Matsubara
| Royal Society of Chemistry Verified
Peptide mimotopes to emulate carbohydrates† Teruhiko Matsubara a Abstract Glycoconjugates on animal cell surfaces are involved in numerous biological functions and diseases, especially the adhesion/metastasis of cancer cells, infection, and the onset of glycan-related diseases. In addition to glycoantigen detection, the regulation of glycan (carbohydrate)–protein interactions is needed to develop therapeutic strategies for glycan-related diseases.
Open in Who Shared Issue with article?

Amyloid-β fibrils assembled on ganglioside-enriched membranes contain both parallel β-sheets and turns

|
By Teruhiko Matsubara, Hanaki Yasumori, Koichiro Ito, Takafumi Shimoaka
| The Journal of Biological Chemistry Verified
Some protein and peptide aggregates, such as those of amyloid-β protein (Aβ), are neurotoxic and have been implicated in several neurodegenerative diseases. Aβ accumulates at nanoclusters enriched in neuronal lipids called gangliosides in the presynaptic neuronal membrane, and the resulting oligomeric and/or fibrous forms accelerate the development of Alzheimer's disease.
Open in Who Shared Issue with article?
See all 5 articles