enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Unfolded protein response - Wikipedia

    en.wikipedia.org/wiki/Unfolded_protein_response

    The unfolded protein response (UPR) is a cellular stress response related to the endoplasmic reticulum (ER) stress. [1] It has been found to be conserved between mammalian species, [2] as well as yeast [1] [3] and worm organisms. The UPR is activated in response to an accumulation of unfolded or misfolded proteins in the lumen of the

  3. Endoplasmic reticulum - Wikipedia

    en.wikipedia.org/wiki/Endoplasmic_reticulum

    The endoplasmic reticulum is found in most eukaryotic cells and forms an interconnected network of flattened, membrane-enclosed sacs known as cisternae (in the RER), and tubular structures in the SER. The membranes of the ER are continuous with the outer nuclear membrane. The endoplasmic reticulum is not found in red blood cells, or spermatozoa.

  4. Membrane contact site - Wikipedia

    en.wikipedia.org/wiki/Membrane_contact_site

    PM-ER contact sites have a well known role in the control of calcium dynamics. The major intracellular pool of calcium is the ER and its release may be triggered by different stimuli. In excitable cells the coupling between PM depolarization and the release from the intracellular pools is essential to generate the Ca 2+ signalling.

  5. Endoplasmic-reticulum-associated protein degradation - Wikipedia

    en.wikipedia.org/wiki/Endoplasmic-reticulum...

    HIV uses an efficient mechanism to dislocate a single-membrane-spanning host protein, CD4, from the ER and submits it to ERAD. The Vpu protein of HIV-1 is a protein on the ER membrane and targets newly made CD4 in the endoplasmic reticulum for degradation by cytosolic proteasomes. [3] Vpu only utilizes part of the ERAD process to degrade CD4.

  6. Nicotinamide adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Nicotinamide_adenine_di...

    In this diagram, the hydride acceptor C4 carbon is shown at the top. When the nicotinamide ring lies in the plane of the page with the carboxy-amide to the right, as shown, the hydride donor lies either "above" or "below" the plane of the page. If "above" hydride transfer is class A, if "below" hydride transfer is class B. [56]

  7. ER diagram - Wikipedia

    en.wikipedia.org/?title=ER_diagram&redirect=no

    This page was last edited on 23 May 2012, at 03:06 (UTC).; Text is available under the Creative Commons Attribution-ShareAlike 4.0 License; additional terms may apply ...

  8. Glycosylation - Wikipedia

    en.wikipedia.org/wiki/Glycosylation

    The N-linked glycosylation process occurs in eukaryotes in the lumen of the endoplasmic reticulum and widely in archaea, but very rarely in bacteria. In addition to their function in protein folding and cellular attachment, the N-linked glycans of a protein can modulate a protein's function, in some cases acting as an on/off switch.

  9. Chaperone (protein) - Wikipedia

    en.wikipedia.org/wiki/Chaperone_(protein)

    In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation.