Results 111 to 120 of about 13,634 (224)

The purification of early-pregnancy factor to homogeneity from human platelets and identification as chaperonin 10

, 1994
Early-pregnancy factor (EPF), first discovered in the early stages of gestation, is associated with and necessary for cell proliferation in a wide variety of biological situations.
Cavanagh A.C., Morton H.
core   +1 more source

Small molecule modulation of HSP60/10 chaperonin systems: More common than previously thought?

, 2019
All living organisms contain a unique class of molecular chaperones called 60 kilodalton heat shock proteins (HSP60, also known as GroEL in bacteria).
Chapman, Eli, Chitre, Siddhi, Johnson, Steven, Salim, Nilshad, Park, Yangshin, Abdeen, Sanofar, Ray, Anne-Marie, Stevens, Mckayla, Washburn, Alex, Sivinski, Jared, Hoang, Quyen   +10 more
core  

Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly. [PDF]

The mitochondrial chaperonin, mitochondrial heat shock protein 60 (mtHsp60), promotes the folding of newly imported and transiently misfolded proteins in the mitochondrial matrix, assisted by its co-chaperone mtHsp10.
Braxton, Julian, Shao, Hao, Gestwicki, Jason, Southworth, Daniel, Tse, Eric   +4 more
core   +1 more source

Mechanism of substrate recognition by the chaperonin GroEL

, 2001
The bacterial chaperonin GroEL functions with its cofactor GroES in assisting the folding of a wide range of proteins in an ATP-dependent manner. GroEL–GroES constitute one of the main chaperone systems in the Escherichia coli cytoplasm.
Walid A Houry
core   +1 more source

Correction: Chaperonin 60 sustains osteoblast autophagy and counteracts glucocorticoid aggravation of osteoporosis by chaperoning RPTOR. [PDF]

Cell Death Dis, 2019
Lian WS, Ko JY, Chen YS, Ke HC, Wu SL, Kuo CW, Wang FS.   +6 more
europepmc   +1 more source

Structural investigation of the molecular chaperonin TF55 from the thermophilic archeon Sulfolobus solfataricus

, 2014
Chaperonins are ubiquitous multi-subunit macromolecules that mediate the folding and assembly of certain proteins that cannot fold properly in vivo. The Archaea bacterium Sulfolobus solfataricus encodes for three chaperonin complexes formed from three ...
Molugu, Sanjay Kumar
core  

Structure of Mycobacterium tuberculosis chaperonin-10 at 3.5 Å resolution

, 2002
Chaperonin-60 (cpn60) and chaperonin-10 (cpn10) are essential proteins involved in ATP-dependent folding of several intracellular proteins in the bacterial cell.
Bhupesh Taneja, Taneja, B., Shekhar C. Mande, Mande, S. C.   +3 more
core   +1 more source

Chaperonin 60 sustains osteoblast autophagy and counteracts glucocorticoid aggravation of osteoporosis by chaperoning RPTOR. [PDF]

Cell Death Dis, 2018
Lian WS, Ko JY, Chen YS, Ke HC, Wu SL, Kuo CW, Wang FS.   +6 more
europepmc   +1 more source

Breakdown of articular cartilage by chaperonin 60

International Journal of Experimental Pathology, 1998
J.C. LEWTHWAITE, J. BIRD, A. MILLER, M.T. BAYLISS, B. HENDERSON   +4 more
openaire   +2 more sources

Structure of holo-chaperonin studied with electron microscopy Oligomeric cpn10 on top of two layers of cpn60 rings with two stripes each

, 1992
A structural model of holo-chaperonin, known as a protein-folding control protein comprising 60 kDa (cpn60) and 10 kDa polypeptides (cpn10), is proposed based on the electron microscopic images of holo-chaperonin from Thermus thermophilus and cpn60 from ...
Hideki Taguchi, Masato Sumi, Masasuke Yoshida, Ishii, Noriyuki, Taguchi, Hideki, Noriyuki Ishii, Yoshida, Masasuke, Sumi, Masato   +7 more
core   +1 more source