Results 101 to 110 of about 13,634 (224)

Deconstruction of Stable Cross-Beta Fibrillar Structures into Toxic and Nontoxic Products Using a Mutated Archaeal Chaperonin

open access: yes, 2016
Our group recently determined that a mutant archaeal chaperonin (Hsp 60) exhibited substantially enhanced protein folding activity at low temperatures and was able to deconstruct refractory protein aggregates.
Frank T. Robb (1908748)   +4 more
core   +1 more source

Ordered Nanostructures Made Using Chaperonin Polypeptides

open access: yes, 2004
A recently invented method of fabricating periodic or otherwise ordered nanostructures involves the use of chaperonin polypeptides. The method is intended to serve as a potentially superior and less expensive alternative to conventional lithographic ...
Paavola, Chad   +4 more
core   +1 more source

Localization of the Binding Site of an Antibody Affecting ATPase Activity of Chaperonin cpn60 from Bordetella pertussis

open access: yes, 1993
Image processing has revealed the attachment site of antibody 54G8 on chaperonin 60 (cpn60) from Bordetella pertussis. This antibody, previously shown to affect the ability of chaperonin 10 (cpn10) to inhibit the ATPase activity of cpn60, is attached at ...
Cejka, Z.   +3 more
core   +1 more source

TAHAP AWAL PENGEMBANGAN DETEKSI TUBERKULOSIS BERBASIS PEPTIDA CHAPERONIN 60 DARI Mycobacterium tuberculosis

open access: yes, 2014
Penelitian ini bertujuan untuk mengetahui kemampuan imunoreaktivitas peptida chaperonin 60.1 dan 60.2 Mycobacterium tuberculosis sebagai antigen untuk mendeteksi TB aktif BTA negatifTuberkulosis (TB) di Indonesia merupakan masalah besar.
Ika, Yusticia   +2 more
core  

Studies of the Escherichia coli Chaperonin Protein GroEL (cpn 60) [PDF]

open access: yes, 1994
The reaction of the E.coli chaperonin GroEL (cpn 60) with the ATP analogue 2', 3' oxidised ATP (oATP) was studied with a view to identify the important amino acid(s) present at the ATP binding site of GroEL.
Thomson, Graeme James
core  

Helicobacter pylori secretes the chaperonin GroEL (HSP60), which binds iron

open access: yes, 2013
Helicobacter pylori is a bacterium that can use multiple iron sources. However, it is unknown whether this bacterium secretes molecules such as siderophores or haemophores to scavenge iron.
Norma Velázquez‐Guadarrama   +7 more
core   +1 more source

Bacterial expression and purification of Interleukin-2 Tyrosine kinase: Single step separation of the chaperonin impurity

open access: yes, 2008
Biochemical and biophysical characterization of kinases requires large quantities of purified protein. Here we report the bacterial expression and purification of active Itk kinase domain (a Tec family kinase) using ArcticExpress cells that co-express ...
Andreotti, Amy, Joseph, Raji
core   +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

Molecular characterisation of the Xenopus laevis chaperonin gene Cctg

open access: yes, 1996
By library screening and PCR we have obtained cDNA clones which encode the gamma subunit of the CCT chaperonin complex fromXenopus laevis. The gene (XlCctg), which encodes the CCTγ subunit contains an open reading frame which codes for 547 amino acid ...
Malik, Afshan   +5 more
core   +1 more source

Mitochondrial chaperonin HSP60 is the apoptosis-related target for myrtucommulone

open access: yes, 2017
The acylphloroglucinol myrtucommulone A (MC) causes mitochondrial dysfunctions by direct interference leading to apoptosis in cancer cells, but the molecular targets involved are unknown.
Katja Wiechmann   +13 more
core   +1 more source

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