Song J
Int J Mol Sci. 2024; 25(23).
PMID: 39684527
PMC: 11641266.
DOI: 10.3390/ijms252312817.
Litberg T, Horowitz S
ACS Chem Biol. 2024; 19(4):809-823.
PMID: 38477936
PMC: 11149768.
DOI: 10.1021/acschembio.3c00695.
Park C, Han B, Choi Y, Jin Y, Kim K, Choi S
RNA Biol. 2024; 21(1):1-18.
PMID: 38361426
PMC: 10878026.
DOI: 10.1080/15476286.2024.2315383.
Litberg T, Sannapureddi R, Huang Z, Son A, Sathyamoorthy B, Horowitz S
RNA Biol. 2023; 20(1):495-509.
PMID: 37493593
PMC: 10373610.
DOI: 10.1080/15476286.2023.2228572.
Son A, Huizar Cabral V, Huang Z, Litberg T, Horowitz S
Proc Natl Acad Sci U S A. 2023; 120(20):e2216308120.
PMID: 37155907
PMC: 10194009.
DOI: 10.1073/pnas.2216308120.
Quantitative reconstitution of yeast RNA processing bodies.
Currie S, Xing W, Muhlrad D, Decker C, Parker R, Rosen M
Proc Natl Acad Sci U S A. 2023; 120(14):e2214064120.
PMID: 36972455
PMC: 10083542.
DOI: 10.1073/pnas.2214064120.
Substoichiometric action of long noncoding RNAs.
Unfried J, Ulitsky I
Nat Cell Biol. 2022; 24(5):608-615.
PMID: 35562482
DOI: 10.1038/s41556-022-00911-1.
RNA multimerization as an organizing force for liquid-liquid phase separation.
Bevilacqua P, Williams A, Chou H, Assmann S
RNA. 2021; 28(1):16-26.
PMID: 34706977
PMC: 8675289.
DOI: 10.1261/rna.078999.121.
RNA as the stone guest of protein aggregation.
Louka A, Zacco E, Temussi P, Tartaglia G, Pastore A
Nucleic Acids Res. 2020; 48(21):11880-11889.
PMID: 33068411
PMC: 7708036.
DOI: 10.1093/nar/gkaa822.
G-Quadruplexes act as sequence-dependent protein chaperones.
Begeman A, Son A, Litberg T, Wroblewski T, Gehring T, Huizar Cabral V
EMBO Rep. 2020; 21(10):e49735.
PMID: 32945124
PMC: 7534610.
DOI: 10.15252/embr.201949735.
Enzymatic degradation of RNA causes widespread protein aggregation in cell and tissue lysates.
Aarum J, Cabrera C, Jones T, Rajendran S, Adiutori R, Giovannoni G
EMBO Rep. 2020; 21(10):e49585.
PMID: 32945072
PMC: 7534620.
DOI: 10.15252/embr.201949585.
Chaperna: linking the ancient RNA and protein worlds.
Son A, Horowitz S, Seong B
RNA Biol. 2020; 18(1):16-23.
PMID: 32781880
PMC: 7834078.
DOI: 10.1080/15476286.2020.1801199.
A widespread family of heat-resistant obscure (Hero) proteins protect against protein instability and aggregation.
Tsuboyama K, Osaki T, Matsuura-Suzuki E, Kozuka-Hata H, Okada Y, Oyama M
PLoS Biol. 2020; 18(3):e3000632.
PMID: 32163402
PMC: 7067378.
DOI: 10.1371/journal.pbio.3000632.
Dynamic conformational flexibility and molecular interactions of intrinsically disordered proteins.
Bhattarai A, Emerson I
J Biosci. 2020; 45.
PMID: 32020911
Polyanions provide selective control of APC/C interactions with the activator subunit.
Mizrak A, Morgan D
Nat Commun. 2019; 10(1):5807.
PMID: 31862931
PMC: 6925294.
DOI: 10.1038/s41467-019-13864-1.
DNA Facilitates Oligomerization and Prevents Aggregation via DNA Networks.
Litberg T, Docter B, Hughes M, Bourne J, Horowitz S
Biophys J. 2019; 118(1):162-171.
PMID: 31839258
PMC: 6952221.
DOI: 10.1016/j.bpj.2019.11.022.
Biological Pathway Specificity in the Cell-Does Molecular Diversity Matter?.
Walter N
Bioessays. 2019; 41(8):e1800244.
PMID: 31245864
PMC: 6684156.
DOI: 10.1002/bies.201800244.
Stabilization of Intrinsically Disordered DKK2 Protein by Fusion to RNA-Binding Domain.
Lee H, Kwon S, Son A, Kim D, Kim K, Lim J
Int J Mol Sci. 2019; 20(11).
PMID: 31212691
PMC: 6600415.
DOI: 10.3390/ijms20112847.
Rescue of degenerating neurons and cells by stem cell released molecules: using a physiological renormalization strategy.
Maguire G, Paler L, Green L, Mella R, Valcarcel M, Villace P
Physiol Rep. 2019; 7(9):e14072.
PMID: 31050222
PMC: 6497969.
DOI: 10.14814/phy2.14072.
Conversion of a soluble protein into a potent chaperone in vivo.
Kwon S, Ryu K, Son A, Jeong H, Lim K, Kim K
Sci Rep. 2019; 9(1):2735.
PMID: 30804538
PMC: 6389997.
DOI: 10.1038/s41598-019-39158-6.