Results 101 to 110 of about 5,379 (199)

Coexistence of group I and group II chaperonins in the archaeon Methanosarcina mazei

open access: yes, 2003
Two distantly related classes of cylindrical chaperonin complexes assist in the folding of newly synthesized and stress-denatured proteins in an ATP-dependent manner.
Pfeifer, G.   +11 more
core   +1 more source

Increased expression and purification of soluble iron-regulatory protein 1 from Escherichia coli co-expressing chaperonins GroES and GroEL

open access: yesBrazilian Journal of Medical and Biological Research, 2008
Iron is an essential metal for all living organisms. However, iron homeostasis needs to be tightly controlled since iron can mediate the production of reactive oxygen species, which can damage cell components and compromise the integrity and/or cause DNA
H. Carvalho, R. Meneghini
doaj  

Seryl phosphorylation modulates chaperonin function of Mycobacterial chaperonin, Cpn60.1

open access: yesCell Stress & Chaperones
The GroEL chaperonin forms a 14‑subunit double ring that encapsulates client proteins for folding with the aid of the cochaperonin GroES. Mycobacteria encode two GroEL homologs: Cpn60.2 (which is essential) and Cpn60.1 (which is non-essential but which ...
C. M. Santosh Kumar   +3 more
doaj   +1 more source

The Unfolding Story of the Chaperonins [PDF]

open access: yesBiotechnology and Genetic Engineering Reviews, 1999
A R, Coates, B, Henderson, P, Mascagni
openaire   +2 more sources

The Role of the Host Cytoskeleton in the Formation and Dynamics of Rotavirus Viroplasms

open access: yesViruses
Rotavirus (RV) replicates within viroplasms, membraneless electron-dense globular cytosolic inclusions with liquid–liquid phase properties. In these structures occur the virus transcription, replication, and packaging of the virus genome in newly ...
Janine Vetter   +2 more
doaj   +1 more source

Editorial: Type I Chaperonins: Mechanism and Beyond

open access: yesFrontiers in Molecular Biosciences, 2018
Adina Breiman, Abdussalam Azem
doaj   +1 more source

Structure and function of chaperonins, molecular assistants of protein folding [PDF]

open access: yes
Proteins in the cell are routinely exposed to various conditions that promote unfolding and irreversible aggregation. Chaperonins act to prevent protein denaturation and aggregation by sequestering aggregation-prone protein molecules and encouraging ...
カワタ, ヤスシ   +11 more
core   +1 more source

Ancestral Chaperonins Provide the First Structural Glimpse into Early Multimeric Protein Evolution. [PDF]

open access: yesMol Biol Evol
Severino R   +8 more
europepmc   +1 more source

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