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Unraveling the Existence of Different Oligomeric Forms of E. Coli Small Heat-Shock Protein Ibpb Under Heat Stress and the Most Functional Oligomers with Respect to Holding Chaperone Activity

https://doi.org/10.2139/ssrn.4772706
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A review on oligomeric polydispersity and oligomers-dependent holding chaperone activity of the small heat-shock protein IbpB of Escherichia coli
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IbpA and IbpB, the new heat-shock proteins, bind to endogenous Escherichia coli proteins aggregated intracellularly by heat shock
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Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli
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Self-association of a Small Heat Shock Protein
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Distinct Activities of Escherichia coli Small Heat Shock Proteins IbpA and IbpB Promote Efficient Protein Disaggregation
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Two Bacterial Small Heat Shock Proteins, IbpA and IbpB, Form a Functional Heterodimer
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Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions
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Small heat shock proteins, IbpA and IbpB, are involved in resistances to heat and superoxide stresses in Escherichia coli
inferredcites →https://doi.org/10.1016/s0968-0004(97)01171-7openalex-extracted
Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms
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Binding of a chaperonin to the folding intermediates of lactate dehydrogenase
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inferredcites →https://doi.org/10.1038/nsmb993openalex-extracted
Some like it hot: the structure and function of small heat-shock proteins
inferredcites →https://doi.org/10.1042/bj3000717openalex-extracted
Refolding of denatured lactate dehydrogenase by Escherichia coli ribosomes
inferredcites →https://doi.org/10.1046/j.1432-1033.2002.02958.xopenalex-extracted
Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants
inferredcites →https://doi.org/10.1073/pnas.1209565109openalex-extracted
Alternative bacterial two-component small heat shock protein systems
inferredcites →https://doi.org/10.1074/jbc.271.12.7218openalex-extracted
Mycobacterium tuberculosis 16-kDa Antigen (Hsp16.3) Functions as an Oligomeric Structure in Vitro to Suppress Thermal Aggregation
inferredcites →https://doi.org/10.1074/jbc.274.15.9937openalex-extracted
Biochemical Characterization of the Small Heat Shock Protein IbpB from Escherichia coli
inferredcites →https://doi.org/10.1074/jbc.m111.273847openalex-extracted
Importance of N- and C-terminal Regions of IbpA, Escherichia coli Small Heat Shock Protein, for Chaperone Function and Oligomerization
inferredcites →https://doi.org/10.1074/jbc.m412706200openalex-extracted
The Small Heat Shock Protein IbpA of Escherichia coli Cooperates with IbpB in Stabilization of Thermally Aggregated Proteins in a Disaggregation Competent State
inferredcites →https://doi.org/10.1099/00221287-148-6-1757openalex-extracted
The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock
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Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli
inferredcites →https://doi.org/10.1128/mmbr.66.1.64-93.2002openalex-extracted
α-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network
inferredcites →https://doi.org/10.1152/physrev.00023.2010openalex-extracted
Large Potentials of Small Heat Shock Proteins
inferredcites →https://doi.org/10.1186/1475-2859-4-6openalex-extracted
The small heat-shock proteins IbpA and IbpB reduce the stress load of recombinant Escherichia coli and delay degradation of inclusion bodies
inferredcites →https://doi.org/10.1371/journal.pgen.1008479openalex-extracted
Duplicate divergence of two bacterial small heat shock proteins reduces the demand for Hsp70 in refolding of substrates
inferredcites →https://doi.org/10.15252/embj.201593378openalex-extracted
Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding
inferredcites →https://doi.org/10.2174/0929866521666131224094408openalex-extracted
In Vitro Holdase Activity of E. coli Small Heat-Shock Proteins IbpA, IbpB and IbpAB: A Biophysical Study with Some Unconventional Techniques
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The Emerging Role of Heat Shock Factor 1 (HSF1) and Heat Shock Proteins (HSPs) in Ferroptosis
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