Calnexin is a new type of molecular chaperone that interacts with many nascent membrane
and soluble proteins of the secretory pathway. Calnexin is unrelated to molecular …

Calnexin, an endoplasmic reticulum transmembrane protein, represents a new type of
molecular chaperone that selectively associates in a transient fashion with newly synthesized …

The three-dimensional structure of the lumenal domain of the lectin-like chaperone calnexin
determined to 2.9 Å resolution reveals an extended 140 Å arm inserted into a β sandwich …

The ability of the pathogenic fungus Candida albicans to switch from a yeast to a hyphal
morphology in response to external signals is implicated in its pathogenicity. We used glass …

In the yeast Saccharomyces cerevisiae the G‐protein beta gamma subunits have been shown
to trigger downstream events of the pheromone response pathway. We have identified a …

Membrane and secretory proteins cotranslationally enter and are folded in the endoplasmic
reticulum (ER). Misfolded or unassembled proteins are discarded by a process known as ER…

Extracellular signal-regulated protein kinase (ERK, or mitogen-activated protein kinase [MAPK])
regulatory cascades in fungi turn on transcription factors that control developmental …

The human fungal pathogen Candida albicans switches from a budding yeast form to a
polarized hyphal form in response to various external signals. This morphogenetic switching has …

The endoplasmic reticulum is the site of folding, disulfide bond formation, and N-glycosylation
of secretory proteins. Correctly folded proteins are exported from the endoplasmic …

Candida albicans is a dimorphic human pathogen in which the yeast to hyphal switch may
be an important factor in virulence in mammals. This pathogen has recently been shown to …