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- W1968659980 endingPage "129" @default.
- W1968659980 startingPage "122" @default.
- W1968659980 abstract "Calreticulin was first isolated 26 years ago. Since its discovery as a minor Ca(2+)-binding protein of the sarcoplasmic reticulum, the appreciation of its importance has grown, and it is now recognized to be a multifunctional protein, most abundant in the endoplasmic reticulum (ER). The protein has well-recognized physiological roles in the ER as a molecular chaperone and Ca(2+)-signalling molecule. However, it has also been found in other membrane-bound organelles, at the cell surface and in the extracellular environment, where it has recently been shown to exert a number of physiological and pathological effects. Here, we will focus on these less-well-characterized functions of calreticulin." @default.
- W1968659980 created "2016-06-24" @default.
- W1968659980 creator A5052943656 @default.
- W1968659980 creator A5065768536 @default.
- W1968659980 creator A5067325703 @default.
- W1968659980 creator A5071277216 @default.
- W1968659980 date "2001-03-01" @default.
- W1968659980 modified "2023-09-27" @default.
- W1968659980 title "The ins and outs of calreticulin: from the ER lumen to the extracellular space" @default.
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- W1968659980 doi "https://doi.org/10.1016/s0962-8924(01)01926-2" @default.
- W1968659980 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11306273" @default.
- W1968659980 hasPublicationYear "2001" @default.
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