Results 91 to 100 of about 19,683 (209)
GroEL-Proteotyping of Bacterial Communities Using Tandem Mass Spectrometry
, 2023 Profiling bacterial populations in mixed communities is a common task in microbiology. Sequencing of 16S small subunit ribosomal-RNA (16S rRNA) gene amplicons is a widely accepted and functional approach but relies on amplification primers and cannot ...
Myriel Cooper +4 more
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Microbiota Medicine Research, Volume 1, Issue 3, Page 91-106, September 2026.Gut microbiota signatures distinguish chronic constipated patients from healthy individuals, supporting noninvasive diagnostic potential. Despite challenges in identifying psychiatric‐related comorbidities, microbial alterations, particularly in neurotransmitter and inflammatory pathways, lay the groundwork for future companion diagnostics and ...
Hongyan Qi +7 more
wiley +1 more source
Український журнал Здоров'я жінкиМета - встановити рівні анти-HSP60 і анти-GroEL антитіл у сироватці крові вагітних із хронічною гіпертензією та накладеною прееклампсією; оцінити можливість їх використання як предикторів накладеної прееклампсії. Матеріали та методи.
O.K. Popel, D.O. Govsieiev
doaj +1 more source
SAXS profiles of GroEL and Hsp60.
, 2014 SAXS profiles of GroEL (red) and naïve Hsp60 (green). GroEL is at c = 52.5 µM, while Hsp60 is at c = 79.5 µM. Experimental curves are scaled for the sake of clarity.
Donatella Bulone (23133) +19 more
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Seryl phosphorylation modulates chaperonin function of Mycobacterial chaperonin, Cpn60.1
Cell Stress & ChaperonesThe 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
Single-Ring GroEL: An Expanded View [PDF]
, 2006 A remarkable structure of an 86 kDa substrate encapsulated in a single-ring GroEL/GroES chaperonin complex is revealed by cryo-electron microscopy in this issue of Structure (Chen et al., 2006).
Wolf, Sharon Grayer
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Chaperomics: In Vivo GroEL Function Defined [PDF]
Current Biology, 2005 A recent proteome analysis of protein folding inside cells of Escherichia coli predicts that only 84 of the approximately 2400 cytosolic proteins expressed in minimal media depend absolutely on the GroEL/GroES chaperone system to avoid aggregation. These proteins are enriched in alpha/beta domains and 13 are essential for growth.
openaire +2 more sources
, 2017 Chaperonin and cochaperonin, represented by E. coli GroEL and GroES, are essential molecular chaperones for protein folding. The double-ring assembly of GroEL is required to function with GroES, and a single-ring GroEL variant GroELSR forms a stable ...
Lingling Chen +2 more
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Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes
, 1995 The Escherichia coli chaperonin GroEL and its regulator GroES are thought to mediate adenosine triphosphate-dependent protein folding as an asymmetrical complex, with substrate protein bound within the GroEL cylinder.
Dasilva, A. C. R. +14 more
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GroEL: More than Just a Folding Cage [PDF]
, 2006 The chaperonin GroEL has been thought of as an important but passive player in protein folding, providing an encapsulated environment that allows folding to proceed unimpaired by aggregation. In this issue, Tang et al.
Radford, Sheena E.
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