| scholarly article | Q13442814 |
| P2093 | author name string | Ishrat Jahan | |
| Shahid M Nayeem | |||
| P2860 | cites work | PRALINE: a multiple sequence alignment toolbox that integrates homology-extended and secondary structure information | Q24812359 |
| Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features | Q27860675 | ||
| GROMACS: fast, flexible, and free | Q27860998 | ||
| Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins | Q28281645 | ||
| Determination and analysis of urea and guanidine hydrochloride denaturation curves | Q29616644 | ||
| Essential dynamics of proteins | Q29616843 | ||
| Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case | Q30164098 | ||
| Suppression of protein aggregation by L-arginine | Q30319084 | ||
| Ionic liquids as refolding additives: N'-alkyl and N'-(omega-hydroxyalkyl) N-methylimidazolium chlorides | Q30320150 | ||
| Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group. | Q30374762 | ||
| Toward an atomistic description of the urea-denatured state of proteins. | Q30608274 | ||
| A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea | Q30849505 | ||
| Characterization of the protein unfolding processes induced by urea and temperature | Q31139306 | ||
| AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides | Q33275645 | ||
| The effect of urea on the structure of water: a molecular dynamics simulation | Q33541167 | ||
| Simulations of the role of water in the protein-folding mechanism | Q33694936 | ||
| Identifying the amylome, proteins capable of forming amyloid-like fibrils | Q33734407 | ||
| Structural clues to prion replication | Q34322278 | ||
| Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. | Q34403513 | ||
| Structure-immunogenicity relationships of therapeutic proteins | Q35814108 | ||
| Anatomy of energetic changes accompanying urea-induced protein denaturation. | Q36024166 | ||
| Computational models for the prediction of polypeptide aggregation propensity | Q36552509 | ||
| Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects | Q36719963 | ||
| Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding | Q36964255 | ||
| Hacking the code of amyloid formation: the amyloid stretch hypothesis | Q37079411 | ||
| Short protein segments can drive a non-fibrillizing protein into the amyloid state | Q37285515 | ||
| Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid | Q37302673 | ||
| Aqueous urea solution destabilizes Abeta(16-22) oligomers | Q37570941 | ||
| Cosolvent effects on protein stability | Q38072485 | ||
| BSE prions propagate as either variant CJD-like or sporadic CJD-like prion strains in transgenic mice expressing human prion protein | Q39686522 | ||
| The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways | Q41728317 | ||
| Biophysical effect of amino acids on the prevention of protein aggregation | Q44163713 | ||
| Molecular dynamics simulations of end-to-end contact formation in hydrocarbon chains in water and aqueous urea solution | Q44311312 | ||
| The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation | Q44410263 | ||
| Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent | Q44592404 | ||
| Interaction of urea with amino acids: implications for urea-induced protein denaturation | Q46875424 | ||
| Pathologic conformations of prion proteins | Q46894080 | ||
| Exploring Protein Stability by Comparative Molecular Dynamics Simulations of Homologous Hyperthermophilic, Mesophilic, and Psychrophilic Proteins. | Q51462074 | ||
| The PASTA server for protein aggregation prediction. | Q51907234 | ||
| Interactions between hydrophobic and ionic solutes in aqueous guanidinium chloride and urea solutions: lessons for protein denaturation mechanism. | Q51914499 | ||
| Convergence of sampling in protein simulations. | Q52044232 | ||
| Coherent microscopic picture for urea-induced denaturation of proteins. | Q52627346 | ||
| Effect of urea on the β-hairpin conformational ensemble and protein denaturation mechanism. | Q53088094 | ||
| Hydrophobicity at a Janus Interface | Q56873766 | ||
| The same prion strain causes vCJD and BSE | Q57092996 | ||
| An Automated Force Field Topology Builder (ATB) and Repository: Version 1.0 | Q57204661 | ||
| Relationship between structural order and the anomalies of liquid water | Q59066041 | ||
| Protein interactions with urea and guanidinium chloride. A calorimetric study | Q67493188 | ||
| Simulations of proteins in water | Q68756088 | ||
| Similarities between principal components of protein dynamics and random diffusion | Q73344940 | ||
| Do water molecules mediate protein-DNA recognition? | Q77642681 | ||
| THE EFFECT OF COMPOUNDS OF THE UREA-GUANIDINIUM CLASS ON THE ACTIVITY COEFFICIENT OF ACETYLTETRAGLYCINE ETHYL ESTER AND RELATED COMPOUNDS | Q78500310 | ||
| Free energy landscape of a biomolecule in dihedral principal component space: sampling convergence and correspondence between structures and minima | Q79909335 | ||
| L-arginine suppresses aggregation of recombinant growth hormones in refolding process from E. coli inclusion bodies | Q81154135 | ||
| Denaturation and aggregation of lysozyme in water-ethanol solution | Q84407295 | ||
| Molecular dynamics simulation of aqueous urea solution: is urea a structure breaker? | Q85640091 | ||
| Unravelling the Composition-Dependent Anomalies of Pair Hydrophobicity in Water-Ethanol Binary Mixtures | Q88994927 | ||
| P433 | issue | 9 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 11727-11741 | |
| P577 | publication date | 2018-09-30 | |
| P1433 | published in | ACS Omega | Q27727647 |
| P1476 | title | Effect of Urea, Arginine, and Ethanol Concentration on Aggregation of CVNITV Fragment of Sheep Prion Protein | |
| P478 | volume | 3 |
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