Richard N Sifers
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Explore the profile of Richard N Sifers including associated specialties, affiliations and a list of published articles.
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29
Citations
695
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Recent Articles
1.
Sifers R
Cell Chem Biol
. 2023 Jan;
30(1):1-2.
PMID: 36669468
In this issue of Cell Chemical Biology, Sun et al. utilize computational and protein expression analyses, plus pharmacological proteostasis network activation, to simultaneously correct two genetic diseases linked to a...
2.
Sun A, Collette J, Sifers R
Proc Natl Acad Sci U S A
. 2020 Sep;
117(40):24825-24836.
PMID: 32958677
The failure of polypeptides to achieve conformational maturation following biosynthesis can result in the formation of protein aggregates capable of disrupting essential cellular functions. In the secretory pathway, misfolded asparagine...
3.
Bajaj L, Sharma J, di Ronza A, Zhang P, Eblimit A, Pal R, et al.
J Clin Invest
. 2020 Jun;
130(8):4118-4132.
PMID: 32597833
Lysosomal enzymes are synthesized in the endoplasmic reticulum (ER) and transferred to the Golgi complex by interaction with the Batten disease protein CLN8 (ceroid lipofuscinosis, neuronal, 8). Here we investigated...
4.
Wang L, Adamski C, Bondar V, Craigen E, Collette J, Pang K, et al.
Mol Psychiatry
. 2019 Jan;
25(10):2504-2516.
PMID: 30696942
Neurons are sensitive to changes in the dosage of many genes, especially those regulating synaptic functions. Haploinsufficiency of SHANK3 causes Phelan-McDermid syndrome and autism, whereas duplication of the same gene...
5.
Mamrosh J, Lee J, Wagner M, Stambrook P, Whitby R, Sifers R, et al.
Elife
. 2015 Jul;
4:e10084.
PMID: 26205891
No abstract available.
6.
Mamrosh J, Lee J, Wagner M, Stambrook P, Whitby R, Sifers R, et al.
Elife
. 2014 Apr;
3:e01694.
PMID: 24737860
Chronic endoplasmic reticulum (ER) stress results in toxicity that contributes to multiple human disorders. We report a stress resolution pathway initiated by the nuclear receptor LRH-1 that is independent of...
7.
Iannotti M, Figard L, Sokac A, Sifers R
J Biol Chem
. 2014 Mar;
289(17):11844-11858.
PMID: 24627495
Conformation-based disorders are manifested at the level of protein structure, necessitating an accurate understanding of how misfolded proteins are processed by the cellular proteostasis network. Asparagine-linked glycosylation plays important roles...
8.
Pan S, Cheng X, Chen H, Castro P, Ittmann M, Hutson A, et al.
PLoS One
. 2013 Aug;
8(8):e72829.
PMID: 23940818
The MAN1B1 gene product, designated ER alpha-1, 2-mannosidase (ERManI), is an enzyme localized in the Golgi complex of mammalian cells. By functioning as a "gate keeper" to prevent the inappropriate...
9.
Sifers R
Chem Biol
. 2013 Mar;
20(3):298-300.
PMID: 23521788
Because proteostasis networks manage the cellular proteome, their pharmacological manipulation might correct pathologies associated with numerous protein misfolding diseases. In this issue of Chemistry & Biology, Tong Ong and colleagues...
10.
Pan S, Cheng X, Sifers R
Mol Biol Cell
. 2013 Feb;
24(8):1111-21.
PMID: 23427261
Endoplasmic reticulum (ER) α-1, 2-mannosidase (ERManI) contributes to ER-associated protein degradation (ERAD) by initiating the formation of degradation signals on misfolded N-linked glycoproteins. Despite its inferred intracellular location, we recently...