| scholarly article | Q13442814 |
| P50 | author | Mosè Rossi | Q69556253 |
| Rita Casadio | Q28946169 | ||
| P2093 | author name string | Pier Luigi Martelli | |
| Antonietta Giordano | |||
| Carlo A Raia | |||
| P2860 | cites work | Replacing the glutamate ligand in the structural zinc site of Sulfolobus solfataricus alcohol dehydrogenase with a cysteine decreases thermostability | Q43022519 |
| Crystallization and preliminary X-ray analysis of an NAD(+)-dependent alcohol dehydrogenase from the extreme thermophilic archaebacterium Sulfolobus solfataricus | Q43023521 | ||
| Alcohol dehydrogenase from Sulfolobus solfataricus | Q43551701 | ||
| Predictions of protein segments with the same aminoacid sequence and different secondary structure: a benchmark for predictive methods. | Q52072059 | ||
| Asn249Tyr substitution at the coenzyme binding domain activates Sulfolobus solfataricus alcohol dehydrogenase and increases its thermal stability. | Q54102931 | ||
| Role of zinc in horse liver alcohol dehydrogenase. Coenzyme and substrate binding. | Q54153412 | ||
| Protein Crystal Growth in the Advanced Protein Crystallization Facility on the LMS Mission: a Comparison of Sulfolobus solfataricus Alcohol Dehydrogenase Crystals Grown on the Ground and in Microgravity | Q57215355 | ||
| CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice | Q24286950 | ||
| Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family | Q24304464 | ||
| PROCHECK: a program to check the stereochemical quality of protein structures | Q26778411 | ||
| Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features | Q27860675 | ||
| WHAT IF: a molecular modeling and drug design program | Q27860734 | ||
| Comparative protein modelling by satisfaction of spatial restraints | Q27860866 | ||
| RASMOL: biomolecular graphics for all | Q29547757 | ||
| Thermostable NAD(+)-dependent alcohol dehydrogenase from Sulfolobus solfataricus: gene and protein sequence determination and relationship to other alcohol dehydrogenases | Q33195324 | ||
| Use of Dimethyl Suberimidate, a Cross-Linking Reagent, in Studying the Subunit Structure of Oligomeric Proteins | Q33698564 | ||
| Evaluation and improvement of multiple sequence methods for protein secondary structure prediction. | Q33855340 | ||
| Zinc coordination, function, and structure of zinc enzymes and other proteins | Q37946601 | ||
| An aspartate residue in yeast alcohol dehydrogenase I determines the specificity for coenzyme | Q38334413 | ||
| Cloning and overexpression in Escherichia coli of the genes encoding NAD-dependent alcohol dehydrogenase from two Sulfolobus species | Q39839833 | ||
| P433 | issue | 3 | |
| P921 | main subject | Sulfolobus solfataricus | Q3503466 |
| P304 | page(s) | 215-223 | |
| P577 | publication date | 2002-03-01 | |
| P1433 | published in | Protein Engineering Design and Selection | Q15762396 |
| P1476 | title | A low-resolution 3D model of the tetrameric alcohol dehydrogenase from Sulfolobus solfataricus | |
| P478 | volume | 15 |
| Q44752877 | ETD allows for native surface mapping of a 150 kDa noncovalent complex on a commercial Q-TWIMS-TOF instrument |
| Q34348995 | Native electrospray and electron-capture dissociation in FTICR mass spectrometry provide top-down sequencing of a protein component in an intact protein assembly. |
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