English Journal

Drake TM1.
Neuromolecular medicine.Neuromolecular Med.2015 Jun;17(2):147-57. doi: 10.1007/s12017-015-8346-x. Epub 2015 Feb 20.
With the rise of aging populations, new challenges for health care systems are emerging. Degenerative conditions of the central nervous system share a strikingly great deal of similarities, particularly the production and buildup of malfolded proteins. As a result, stress pathways within the endopla
PMID 25697885

C-terminal truncation of a Tat passenger protein affects its membrane translocation by interfering with receptor binding.

Schlesier R, Bernd Klösgen R.
Biological chemistry.Biol Chem.2015 Apr;396(4):349-57. doi: 10.1515/hsz-2014-0249.
During thylakoid transport of the chimeric model twin-arginine translocation (Tat) substrate 16/23, two consecutive translocation intermediates with different membrane topology are observed. The early translocation intermediate Ti-1 is bound to the membrane such that almost half of the protein is pr
PMID 25562604

The interplay of Hrd3 and the molecular chaperone system ensures efficient degradation of malfolded secretory proteins.

Mehnert M1, Sommermeyer F1, Berger M1, Kumar Lakshmipathy S1, Gauss R2, Aebi M2, Jarosch E1, Sommer T3.
Molecular biology of the cell.Mol Biol Cell.2015 Jan 15;26(2):185-94. doi: 10.1091/mbc.E14-07-1202. Epub 2014 Nov 26.
Misfolded proteins of the secretory pathway are extracted from the endoplasmic reticulum (ER), polyubiquitylated by a protein complex termed the Hmg-CoA reductase degradation ligase (HRD-ligase), and degraded by cytosolic 26S proteasomes. This process is termed ER-associated protein degradation (ERA
PMID 25428985

Japanese Journal

Inhibition of Cancer Cell Growth by GRP78 siRNA Lipoplex via Activation of Unfolded Protein Response

Matsumura Kazushi,Sakai Chika,Kawakami Shigeru,Yamashita Fumiyoshi,Hashida Mitsuru
Biological and Pharmaceutical Bulletin 37(4), 648-653, 2014
… Proteasome inhibitors are a novel class of molecular-targeted anti-cancer drugs that suppress the degradation of malfolded proteins, trigger endoplasmic reticulum (ER) stress, and activate apoptosis signals. …
NAID 130003390969

Maifolded Cytochrome P-450(MI) Localized in Unusual Membrane Structures of the Eendoplasmic Reticulum in Cultured Animal Cells

ISHIHARA Naotada,YAMASHINA Shohei,SAKAGUCHI Masao,MIHARA Katsuyoshi,OMURA Tsuneo
The journal of biochemistry 118(2), 397-404, 1995-08-01
NAID 10005445933

Malfolded Cytochrome P-450(M1) Localized in Unusual Membrane Structures of the Endoplasmic Reticulum in Cultured Animal Cells.

Ishihara Naotada,Yamashina Shohei,Sakaguchi Masao,Mihara Katsuyoshi,Omura Tsuneo
The Journal of Biochemistry 118(2), 397-404, 1995
A conserved region containing three to five proline residues is present just behind the signal-anchor sequence in the amino terminal portion of most microsomal cytochrome P-450s. We have shown that th …
NAID 130003532610