| scholarly article | Q13442814 |
| P6179 | Dimensions Publication ID | 1052397074 |
| P356 | DOI | 10.1038/NBT1098-955 |
| P698 | PubMed publication ID | 9788353 |
| P5875 | ResearchGate publication ID | 13498721 |
| P50 | author | Franz X. Schmid | Q62056389 |
| P2093 | author name string | Plückthun A | |
| Sieber V | |||
| P2860 | cites work | Protein engineering from a bioindustrial point of view | Q56902984 |
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| Potential use of additivity of mutational effects in simplifying protein engineering | Q27733698 | ||
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| 15 Libraries of peptides and proteins displayed on filamentous phage | Q36695669 | ||
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| Selectively infective phage (SIP) technology: a novel method for in vivo selection of interacting protein-ligand pairs | Q36864275 | ||
| 3D structural information as a guide to protein engineering using genetic selection | Q36877977 | ||
| Characterization of cspB, a Bacillus subtilis inducible cold shock gene affecting cell viability at low temperatures | Q38325555 | ||
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| SOME PHYSICAL-CHEMICAL AND BIOLOGICAL PROPERTIES OF THE ROD-SHAPED COLIPHAGE M13. | Q44788097 | ||
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| Phage display of proteins | Q56897145 | ||
| P433 | issue | 10 | |
| P304 | page(s) | 955-960 | |
| P577 | publication date | 1998-10-01 | |
| P1433 | published in | Nature Biotechnology | Q1893837 |
| P1476 | title | Selecting proteins with improved stability by a phage-based method | |
| P478 | volume | 16 |
| Q46037815 | A pH-dependent computational approach to the effect of mutations on protein stability. |
| Q80427731 | Aggregation-resistant domain antibodies selected on phage by heat denaturation |
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| Q31162655 | An intein-based genetic selection allows the construction of a high-quality library of binary patterned de novo protein sequences |
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| Q54679413 | Characterisation of a DNA polymerase highly mutated along the template binding interface. |
| Q33197432 | Combinatorial approaches to novel proteins |
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| Q56873918 | Continuous directed evolution of proteins with improved soluble expression |
| Q94563264 | De novo development of proteolytically resistant therapeutic peptides for oral administration |
| Q47577422 | Detection of protein folding defects caused by BRCA1-BRCT truncation and missense mutations |
| Q46420501 | Directed evolution of an extremely stable fluorescent protein. |
| Q31113507 | Directed evolution of barnase stability using proteolytic selection |
| Q33533813 | Directed evolution of biocatalysts |
| Q47253797 | Directed evolution to improve protein folding in vivo |
| Q90215505 | Engineered peptide barcodes for in-depth analyses of binding protein libraries |
| Q28478199 | Engineered single-domain antibodies with high protease resistance and thermal stability |
| Q27687991 | Engineering protein thermostability using a generic activity-independent biophysical screen inside the cell |
| Q31141217 | Evolutionary Stabilization of the Gene-3-protein of Phage fd Reveals the Principles that Govern the Thermodynamic Stability of Two-domain Proteins |
| Q38713206 | Exploiting sequence and stability information for directing nanobody stability engineering. |
| Q30890462 | FRET-based in vivo screening for protein folding and increased protein stability |
| Q54454392 | Formation of active inclusion bodies in the periplasm of Escherichia coli. |
| Q34528019 | Generating thermal stable variants of protein domains through phage display |
| Q33185813 | Genetic screens and directed evolution for protein solubility |
| Q38680071 | Global analysis of protein folding using massively parallel design, synthesis, and testing |
| Q30799638 | High-affinity fragment complementation of a fibronectin type III domain and its application to stability enhancement |
| Q33357098 | High-throughput analysis of the protein sequence-stability landscape using a quantitative yeast surface two-hybrid system and fragment reconstitution |
| Q34954888 | Highly diverse protein library based on the ubiquitous (β/α)₈ enzyme fold yields well-structured proteins through in vitro folding selection |
| Q50892018 | How do miniproteins fold? |
| Q31908651 | Improving the display of proteins on filamentous phage |
| Q34729557 | In vitro evolution of glutathione S-transferase using a plasmid display system based on the GAL4 DNA-binding domain |
| Q34070107 | In vitro selection and evolution of proteins |
| Q30978988 | In vitro selection for enzymatic activity: a model study using adenylate cyclase |
| Q30428175 | Initiation of phage infection by partial unfolding and prolyl isomerization |
| Q35545646 | Intra-domain phage display (ID-PhD) of peptides and protein mini-domains censored from canonical pIII phage display |
| Q37862655 | Lessons about protein stability from in vitro selections |
| Q36525476 | Lessons in stability from thermophilic proteins |
| Q27008422 | Library methods for structural biology of challenging proteins and their complexes |
| Q33949042 | Library-based methods for identification of soluble expression constructs |
| Q30980912 | Mirror-image phage display: aiming at the mirror |
| Q38109676 | Modulating protein stability - directed evolution strategies for improved protein function |
| Q33241335 | Modulation of infectivity in phage display as a tool to determine the substrate specificity of proteases |
| Q44099828 | Molecular modification of Protein A to improve the elution pH and alkali resistance in affinity chromatography |
| Q30978746 | New understandings of thermostable and peizostable enzymes |
| Q30168811 | Novel folded protein domains generated by combinatorial shuffling of polypeptide segments |
| Q38206516 | Open questions in origin of life: experimental studies on the origin of nucleic acids and proteins with specific and functional sequences by a chemical synthetic biology approach |
| Q34313175 | Optimization of protein solubility and stability for protein nuclear magnetic resonance |
| Q41858624 | Optimizing protein stability in vivo |
| Q31087399 | Origins of the high stability of an in vitro-selected cold-shock protein |
| Q30979228 | Phage display as a tool for the directed evolution of enzymes |
| Q34458172 | Phage selection of cyclic peptide antagonists with increased stability toward intestinal proteases |
| Q41830011 | Probing protein stability and proteolytic resistance by loop scanning: a comprehensive mutational analysis |
| Q46529356 | Prolyl isomerization as a molecular timer in phage infection |
| Q30888974 | Protein stabilization through phage display |
| Q22061732 | Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding |
| Q30648176 | Reaction kinetics of protease with substrate phage. Kinetic model developed using stromelysin |
| Q27639826 | Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography |
| Q28673623 | Refolding of a thermostable glyceraldehyde dehydrogenase for application in synthetic cascade biomanufacturing |
| Q46144677 | SCHEMA-guided protein recombination |
| Q31135914 | Selection based on the folding properties of proteins with ribosome display |
| Q30834821 | Selectively infective phage (SIP) technology: scope and limitations. |
| Q31826132 | Selectively infective phage technology |
| Q36859580 | Some like it hot: the molecular determinants of protein thermostability |
| Q35555979 | Stress selections on domain antibodies: 'what doesn't kill you makes you stronger'. |
| Q89313462 | Structure-Guided Engineering of α-Keto Acid Decarboxylase for the Production of Higher Alcohols at Elevated Temperature |
| Q33696431 | The Case for Trypsin Release of Affinity-Selected Phages |
| Q30914643 | The use of phage display for the development of tumour targeting agents |
| Q35417777 | Thermostable artificial enzyme isolated by in vitro selection |
| Q21045399 | Tying up the loose ends: circular permutation decreases the proteolytic susceptibility of recombinant proteins |
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