Results 31 to 40 of about 27,570 (293)

Structural Plasticity and Noncovalent Substrate Binding in the GroEL Apical Domain. A study using electrospray ionization mass spectrometry and fluorescence binding studies [PDF]

, 2002
Advances in understanding how GroEL binds to non-native proteins are reported. Conformational flexibility in the GroEL apical domain, which could account for the variety of substrates that GroEL binds, is illustrated by comparison of several independent ...
Adams, Boisvert, Braig, Braig, Brinker, Brocchierei, Brunger, Brunger, Buckle, Bukau, Chatellier, Chatellier, Chatellier, Chen, Collaborative Computational Project, N., Coyle, Dessauer, Ewalt, Feltham, Fenton, Ferrige, Grallert, Hartl, Hartl, HayerHartl, Hemmingsen, Hlodan, Houry, Hunt, Hutchinson, Jancarik, Jones, Jones, Kobayashi, Konermann, Kraunsoe, Kusmierczyk, Landry, Landry, Leslie, Loo, Ma, Murshudov, Navaza, Pace, Pflugrath, Ploegman, Raftery, Ranson, Robinson, Romano, Roseman, Rye, Sigler, Smith, Smote, Tanaka, Wang, Weber, Weber, Weissman, Xu, Zahn   +62 more
core   +1 more source

Exposure of Bifidobacterium longum subsp. infantis to Milk Oligosaccharides Increases Adhesion to Epithelial Cells and Induces a Substantial Transcriptional Response [PDF]

, 2013
Devon Kavanaugh is in receipt of a Teagasc Walsh Fellowship. The authors would also like to acknowledge the support of Science Foundation Ireland under Grant No.
Butto, Ludovica F., Clyne, Marguerite, Hickey, Rita M., Joshi, Lokesh, Kane, Marian, Kavanaugh, Devon W., Lane, Jonathan, O'Callaghan, John, Slattery, Helen   +8 more
core   +7 more sources

HSP10 as a Chaperone for Neurodegenerative Amyloid Fibrils

Frontiers in Neuroscience, 2022
Neurodegenerative diseases (NDs) are associated with accumulated misfolded proteins (MPs). MPs oligomerize and form multiple forms of amyloid fibril polymorphs that dictate fibril propagation and cellular dysfunction.
Johan N. K. Larsson, Sofie Nyström, Per Hammarström   +2 more
doaj   +1 more source

Information overload in literature [PDF]

, 2016
AHR
Groes, Sebastian
core   +1 more source

Novel Chaperones RrGroEL and RrGroES for Activity and Stability Enhancement of Nitrilase in Escherichia coli and Rhodococcus ruber

Molecules, 2020
For large-scale bioproduction, thermal stability is a crucial property for most industrial enzymes. A new method to improve both the thermal stability and activity of enzymes is of great significance.
Chunmeng Xu, Lingjun Tang, Youxiang Liang, Song Jiao, Huimin Yu, Hui Luo   +5 more
doaj   +1 more source

Environmental stress responses in Lactococcus lactis [PDF]

, 1999
Bacteria can encounter a variety of physical conditions during their life. Bacterial cells are able to survive these (often adverse) conditions by the induction of specific or general protection mechanisms. The lactic acid bacterium Lactococcus lactis is
Kok, Jan,, Sanders, Jan Willem,, Venema, Gerard,   +2 more
core   +3 more sources

Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition

Biomolecules, 2014
Chaperonin GroEL is a complex oligomeric heat shock protein (Hsp60) assisting the correct folding and assembly of other proteins in the cell. An intriguing question is how GroEL folds itself.
Nataliya Ryabova, Victor Marchenkov, Nina Kotova, Gennady Semisotnov   +3 more
doaj   +1 more source

The Mycobacterium tuberculosis sRNA F6 Modifies Expression of Essential Chaperonins, GroEL2 and GroES

Microbiology Spectrum, 2021
Almost 140 years after the identification of Mycobacterium tuberculosis as the etiological agent of tuberculosis, important aspects of its biology remain poorly described.
Joanna Houghton, Angela Rodgers, Graham Rose, Alexandre D’Halluin, Terry Kipkorir, Declan Barker, Simon J. Waddell, Kristine B. Arnvig   +7 more
doaj   +1 more source

GroE is vital for cell-wall synthesis [PDF]

Nature, 1998
Chaperone proteins help other proteins to fold. GroEL, the Escherichia coli form of the ubiquitous Cpn60 chaperonins, has a multimeric barrel-shaped structure with a central cavity, within which almost any protein can fold in vitro1. But what does GroE (GroEL plus its co-chaperone GroES) fold in the cell? Why is it needed for cell survival2?
N, McLennan, M, Masters
openaire   +2 more sources

Stress-related genes promote Edwardsiella ictaluri pathogenesis. [PDF]

PLoS ONE, 2018
Edwardsiella ictaluri is a Gram-negative facultative anaerobic rod and the causative agent of enteric septicemia of channel catfish (ESC), which is one of the most prevalent diseases of catfish, causing significant economic losses in the catfish industry.
Ali Akgul, Ayfer Akgul, Mark L Lawrence, Attila Karsi   +3 more
doaj   +1 more source