Results 91 to 100 of about 20,108 (219)

Visualizing chaperonin function in situ by cryo-electron tomography [PDF]

Chaperonins are large barrel-shaped complexes that mediate ATP-dependent protein folding 1–3 . The bacterial chaperonin GroEL forms juxtaposed rings that bind unfolded protein and the lid-shaped cofactor GroES at their apertures. In vitro analyses of the
Baumeister, Wolfgang, Hartl, F. Ulrich, Beck, Florian, Bohn, Stefan, Wan, William, Wagner, Jonathan, Bracher, Andreas, Körner, Roman, Fernandez-Busnadiego, Ruben, Carvajal, Alonso I.   +9 more
core   +3 more sources

OsCPN10a, cooperating with OsCPN20 and OsHSP60‐3B negatively regulate ABA signaling and enhance seed storability in rice

Journal of Integrative Plant Biology, Volume 68, Issue 7, Page 2242-2263, July 2026.
Abscisic acid signaling homeostasis is essential for seed storability. The molecular chaperone OsCPN10a enhances rice seed storability by forming a trimeric chaperone complex with OsCPN20‐OsHSP60‐3B that attenuates abscisic acid signaling via direct interaction with OsPYL10‐OsABIL1, thereby maintaining starch integrity and offering a promising target ...
Sufeng Liao, Yidong Wei, Yongsheng Zhu, Kunyang Li, Ting Chen, Shuai Zhao, Fangxi Wu, Jinlan Wang, Pengbo Yu, Hongguang Xie, Liping Chen, Qiuhua Cai, Huaan Xie, Jianfu Zhang   +13 more
wiley   +1 more source

Single-molecule spectroscopy of protein folding in a chaperonin cage [PDF]

, 2010
Molecular chaperones are known to be essential for avoiding protein aggregation in vivo, but it is still unclear how they affect protein folding mechanisms.
Nettels, D, Everett A. Lipman, Hagen Hofmann, Daniel Streich, Hoffmann, A, Dominik Haenni, Armin Hoffmann, Haenni, D, Lipman, E A, Streich, D, Frank Hillger, Daniel Nettels, Pfeil, S H, Shawn H. Pfeil, Benjamin Schuler, Hofmann, H, Schuler, B, Hillger, F   +17 more
core   +1 more source

Decoding GUN1 in plastid‐to‐nucleus signaling: what it doesn't, what it does, and why it matters

New Phytologist, Volume 251, Issue 1, Page 81-88, July 2026.
Publication history of plant GUN1 research. Summary Plastid‐to‐nucleus retrograde signaling coordinates nuclear gene expression with the developmental and physiological state of plastids. GENOMES UNCOUPLED 1 (GUN1), a chloroplast‐localized PPR‐SMR protein, remains a central yet poorly understood component of this network.
Marco Wendler, Dario Leister, Tatjana Kleine   +2 more
wiley   +1 more source

The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro. [PDF]

, 1994
We have isolated a chaperonin from the hyperthermophilic archaeon Sulfolobus solfataricus based on its ability to inhibit the spontaneous refolding 5a0t "C of dimeric S. solfataricus malic enzyme.
ROSSI M., CERCHIA L., BARTOLUCCI, SIMONETTA, GUAGLIARDI A.   +3 more
core   +1 more source

Crystal Structure of Chaperonin GroEL from Xanthomonas oryzae pv. oryzae

Crystals, 2019
Xanthomonas oryzae pv. oryzae (Xoo) is a plant pathogen that causes bacterial blight of rice, with outbreaks occurring in most rice-growing countries. Thus far, there is no effective pesticide against bacterial blight.
Huyen-Thi Tran, Jongha Lee, Hyunjae Park, Jeong-Gu Kim, Seunghwan Kim, Yeh-Jin Ahn, Lin-Woo Kang   +6 more
doaj   +1 more source

Structural and functional investigation of Φ-EL-chaperonin mediated protein folding [PDF]

, 2011
Chaperonins are ubiquitous, sequence related protein complexes that aid in the folding of nascent and misfolded polypeptides in an ATP driven pathway. Recently a GroEL-like, 860 kilo Dalton chaperonin protein complex was identified and isolated from the ...
Molugu, Sudheer Kumar
core   +1 more source

Crystal Structure of the 65 Kilodalton Heat Shock Protein, Chaperonin 60.2, of Mycobacterium tuberculosis [PDF]

, 2004
Chaperonin 60s are a ubiquitous class of proteins that promote folding and assembly of other cellular polypeptides in an ATP dependent manner. The oligomeric state of chaperonin 60s has been shown to be crucial to their role as molecular chaperones ...
Qamra, R., Mande, S.C.
core   +1 more source

The Chaperonin TRiC/CCT Inhibitor HSF1A Protects Cells from Intoxication with Pertussis Toxin

Toxins
Pertussis toxin (PT) is a bacterial AB5-toxin produced by Bordetella pertussis and a major molecular determinant of pertussis, also known as whooping cough, a highly contagious respiratory disease.
Jinfang Jia, Manuel Zoeschg, Holger Barth, Arto T. Pulliainen, Katharina Ernst   +4 more
doaj   +1 more source

Dual Function of Protein Confinement in Chaperonin-assisted Protein Folding [PDF]

, 2001
The GroEL/GroES chaperonin system mediates the folding of a range of newly synthesized polypeptides in the bacterial cytosol. Using a rapid biotin-streptavidin-based inhibition of chaperonin function, we show that the cage formed by GroEL and its ...
Brinker, Achim, Hartl, F.Ulrich, Naylor, D., Kerner, M.J., Brinker, A., Naylor, Dean J., Pfeifer, G., Hayer-Hartl, Manajit, Hayer-Hartl, M., Pfeifer, Guenther, Kerner, M., Naylor, D.J., Kerner, Michael J., Hayer-Hartl, M. K., Hartl, F. U., Hartl, F.   +15 more
core   +1 more source