scholarly article | Q13442814 |
P50 | author | Tomohiro Mizobata | Q58197925 |
P2093 | author name string | Yasushi Kawata | |
Kunihiro Hongo | |||
Yumi Uemura | |||
Shiori Miyawaki | |||
P2860 | cites work | HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria | Q27620904 |
Salt Bridges Regulate Both Dimer Formation and Monomeric Flexibility in HdeB and May Have a Role in Periplasmic Chaperone Function | Q27675931 | ||
Crystal structure of Escherichia coli HdeA | Q27765274 | ||
UCSF Chimera--a visualization system for exploratory research and analysis | Q27860666 | ||
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Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy | Q30375263 | ||
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Escherichia coli HdeB is an acid stress chaperone | Q33262736 | ||
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Acid resistance in enteric bacteria | Q34522511 | ||
A consensus method for the prediction of 'aggregation-prone' peptides in globular proteins | Q34552231 | ||
HdeB functions as an acid-protective chaperone in bacteria | Q34801763 | ||
Chaperone activation by unfolding | Q36747696 | ||
Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding | Q37138591 | ||
Comparative proteomics reveal distinct chaperone-client interactions in supporting bacterial acid resistance | Q37304876 | ||
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A simple algorithm locates beta-strands in the amyloid fibril core of alpha-synuclein, Abeta, and tau using the amino acid sequence alone | Q42276744 | ||
Function of the Escherichia coli nucleoid protein, H-NS: molecular analysis of a subset of proteins whose expression is enhanced in a hns deletion mutant | Q42620591 | ||
Identification of sigma S-dependent genes associated with the stationary-phase acid-resistance phenotype of Shigella flexneri | Q42642088 | ||
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Gly192 at hinge 2 site in the chaperonin GroEL plays a pivotal role in the dynamic apical domain movement that leads to GroES binding and efficient encapsulation of substrate proteins. | Q46171077 | ||
The cytotoxic Staphylococcus aureus PSMα3 reveals a cross-α amyloid-like fibril | Q46519937 | ||
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Helix-turn-helix peptides that form alpha-helical fibrils: turn sequences drive fibril structure | Q46710597 | ||
Conserved amphiphilic feature is essential for periplasmic chaperone HdeA to support acid resistance in enteric bacteria | Q46756313 | ||
The Mechanism of HdeA Unfolding and Chaperone Activation. | Q47402766 | ||
Characterizations of the Interactions between Escherichia coli Periplasmic Chaperone HdeA and Its Native Substrates during Acid Stress | Q47584305 | ||
Identification of amyloid fibril-forming segments based on structure and residue-based statistical potential | Q48395064 | ||
Modulating the Effects of the Bacterial Chaperonin GroEL on Fibrillogenic Polypeptides through Modification of Domain Hinge Architecture. | Q51138141 | ||
Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation. | Q51456848 | ||
Consensus prediction of amyloidogenic determinants in amyloid fibril-forming proteins. | Q51915749 | ||
Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation. | Q52333975 | ||
BeStSel: a web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra. | Q55518831 | ||
Why Study Functional Amyloids? Lessons from the Repeat Domain of Pmel17 | Q57279416 | ||
Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films | Q68581487 | ||
Fluorescent stains, with special reference to amyloid and connective tissues | Q79295401 | ||
P433 | issue | 5 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Escherichia coli | Q25419 |
P304 | page(s) | 1590-1601 | |
P577 | publication date | 2018-12-10 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Acid-denatured small heat shock protein HdeA from Escherichia coli forms reversible fibrils with an atypical secondary structure | |
P478 | volume | 294 |
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