Adam M. Benham
Durham University
51 Papers
477 Citations
Adam M. Benham is an academic researcher from Durham University. The author has contributed to research in topics: Endoplasmic reticulum & Protein disulfide-isomerase. The author has an hindex of 24, co-authored 50 publications. Previous affiliations of Adam M. Benham include University of London & Osaka University.
Chat about Author
Papers
Fertilization: a sperm’s journey to and interaction with the oocyte
TL;DR: The results indicate that what has been observed in in vitro fertilization (IVF) differs significantly from what occurs during "physiological" fertilization.
Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male fertility
TL;DR: Findings reveal that ADAM3 requires testis-specific private chaperones to be folded properly and that the principle role of ADAM2 is for sperm migration into the oviduct but not for the fertilization event, and the importance of primary sperm ZP binding should be reconsidered.
157
Calsperin is a testis specific chaperone required for sperm fertility
Masahito Ikawa,Keizo Tokuhiro,Ryo Yamaguchi,Adam M. Benham,Adam M. Benham,Taku Tamura,Ikuo Wada,Yuhkoh Satouh,Naokazu Inoue,Masaru Okabe +9 more
TL;DR: This work shows that Calr3−/− males produced apparently normal sperm but were infertile because of defective sperm migration from the uterus into the oviduct and defective binding to the zona pellucida, and establishes the client specificity of CALR3.
152
The proteasome-specific inhibitor lactacystin blocks presentation of cytotoxic T lymphocyte epitopes in human and murine cells.
Vincenzo Cerundolo,Adam M. Benham,Veronique M. Braud,Siddhartha Mukherjee,Keith G. Gould,Beatrice Macino,Jacques Neefjes,Alain Townsend +7 more
TL;DR: It is shown that cells treated with lactacystin fail to present influenza antigens to influenza‐specific CTL, but retain the capacity to present defined epitopes expressed as peptides intracellularly by recombinant vaccinia viruses, demonstrating that proteasome‐dependent degradation plays an important role in the cytosolic generation of CTL epitopes.
141
The CXXCXXC motif determines the folding, structure and stability of human Ero1‐Lα
TL;DR: Ero1‐Lα, the human homolog of Ero1p, exists as a collection of oxidized and reduced forms and covalently binds PDI, and the results demonstrate that this motif is important for protein folding, structural integrity, protein half‐life and the stability of the Ero 1‐L α–PDI complex.
135