Molecular characterization of hCTR1, the human copper uptake protein.
Authors: Eisses John F; Kaplan Jack H;
Journal:J Biol Chem
PubMed ID:12034741
'We have expressed hCTR1, the human copper transporter, in Sf9 cells using a baculovirus-mediated expression system, and we observed greatly enhanced copper uptake. Western blots showed that the protein is delivered to the plasma membrane, where it mediates saturable copper uptake with a K(m) of approximately 3.5 microm. We also ... More
Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3.
Authors: Liemann Susanne; Chandran Kartik; Baker Timothy S; Nibert Max L; Harrison Stephen C;
Journal:Cell
PubMed ID:11832217
Cell entry by nonenveloped animal viruses requires membrane penetration without membrane fusion. The reovirus penetration agent is the outer-capsid protein, Mu1. The structure of Mu1, complexed with its ... More
Molecular characterization of major cat allergen Fel d 1: expression of heterodimer by use of a baculovirus expression system.
Fel d 1 is a major cat allergen inducing allergic rhinitis and asthma in sensitized individuals. It has a more complex structure when compared with other allergens and therefore expression of recombinant Fel d 1 has been considered a challenge. The present study shows for the first time that a ... More
A novel 43-kDa protein as a negative regulatory component of phenoloxidase-induced melanin synthesis.
Authors:Zhao M, Söderhäll I, Park JW, Ma YG, Osaki T, Ha NC, Wu CF, Söderhäll K, Lee BL,
Journal:J Biol Chem
PubMed ID:15857824
The melanization reaction induced by activated phenoloxidase in arthropods is important in the multiple host defense innate immune reactions, leading to the sequestration and killing of invading microorganisms. This reaction ought to be tightly controlled because excessive formation of quinones and systemic hypermelanization are deleterious to the hosts, suggesting that ... More
Human MutY homolog, a DNA glycosylase involved in base excision repair, physically and functionally interacts with mismatch repair proteins human MutS homolog 2/human MutS homolog 6.
Authors: Gu Yesong; Parker Antony; Wilson Teresa M; Bai Haibo; Chang Dau-Yin; Lu A-Lien;
Journal:J Biol Chem
PubMed ID:11801590
Adenines mismatched with guanines or 7,8-dihydro-8-oxo-deoxyguanines that arise through DNA replication errors can be repaired by either base excision repair or mismatch repair. The human MutY homolog (hMYH), a DNA glycosylase, removes adenines from these mismatches. Human MutS homologs, hMSH2/hMSH6 (hMutSalpha), bind to the mismatches and initiate the repair on ... More