| 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 |
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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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| 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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