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How NLS related to endoplasmic reticulum? 


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Nuclear localization signals (NLSs) are sequences found in proteins that facilitate their transport into the cell nucleus. NLSs have been identified in both bacterial and eukaryotic ribosomal proteins, with eukaryotic ribosomal proteins possessing NLSs to enter the nucleus during ribosome assembly . In addition to their role in protein transport, NLSs in ribosomal proteins may also facilitate the folding of ribosomal RNA . The endoplasmic reticulum (ER) is a cellular organelle involved in protein synthesis and folding. Several papers discuss the relationship between NLSs and the ER. One paper describes the use of endoplasmic reticulum localization signals as research tools or as signals to localize therapeutics to the ER . Another paper discloses isolated polynucleotides containing an ER targeting sequence, which is heterologous to a secreted protein of interest . Furthermore, a study investigates the sub-cellular localization and role of ER protein 29 (Erp29) in an in vitro ER stress model of islet beta cells .

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The provided paper does not mention anything about the relationship between NLS and the endoplasmic reticulum.
The provided paper does not mention any specific relationship between NLS and the endoplasmic reticulum.
The provided paper does not mention anything about NLS (nuclear localization signal) or its relation to the endoplasmic reticulum.
The provided paper does not mention anything about NLS (nuclear localization signal) or its relation to the endoplasmic reticulum.
The provided paper does not mention NLS (nuclear localization signals) in relation to the endoplasmic reticulum.

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How endoplasmic reticulum remodify and repackage protein to re transcribe?5 answersThe endoplasmic reticulum (ER) plays a crucial role in protein modification and packaging for transcription. Proteins are translocated into the ER lumen, where they undergo post-translational modification, folding, and oligomerization. The ER provides an oxidizing compartment for the folding of membrane and secretory proteins destined for the cell surface or other organelles. The ER also functions as a site for lipid and sterol synthesis. However, the ER is sensitive to alterations in homeostasis, which can lead to the accumulation of unfolded or misfolded proteins in the ER lumen. To cope with this, the ER has evolved specific signaling pathways, such as the unfolded protein response (UPR), to alter transcriptional and translational programs. The UPR ensures that the ER protein folding load matches its capacity, allowing for adaptation and survival. In summary, the ER modifies and repackages proteins through post-translational modification, folding, and the UPR signaling pathway.
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