The DOI matches its Crossref record; 104 of the 104 references it cites were found in a registry or an index.
De Novo Design of Helical Bundles as Models for Understanding Protein Folding and Function
Open accessAbstract
De novo protein design has proven to be a powerful tool for understanding protein folding, structure, and function. In this Account, we highlight aspects of our research on the design of dimeric, four-helix bundles. Dimeric, four-helix bundles are found throughout nature, and the history of their design in our laboratory illustrates our hierarchic approach to protein design. This approach has been successfully applied to create a completely native-like protein. Structural and mutational analysis allowed us to explore the determinants of native protein structure. These determinants were then applied to the design of a dinuclear metal-binding protein that can now serve as a model for this important class of proteins.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Novel Proteinaceous Infectious Particles Cause Scrapie
Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,118
Dominant forces in protein folding
Dill, K. A. (1990) · Biochemistry · doi:10.1021/bi00483a001 · Cited by 3,800
Sickle Cell Anemia, a Molecular Disease
Pauling, L., Itano, H. A., Singer, S. J., & Wells, I. C. (1949) · Science · doi:10.1126/science.110.2865.543 · Cited by 2,319
Protein misfolding, evolution and disease
Dobson, C. M. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01445-0 · Cited by 1,952
The CBP co-activator is a histone acetyltransferase
Bannister, A. J., & Kouzarides, T. (1996) · Nature · doi:10.1038/384641a0 · Cited by 1,805
Creighton, T. E. (1992) · Cited by 1,583
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
Harbury, P. B., Zhang, T., Kim, P. S., & Alber, T. (1993) · Science · doi:10.1126/science.8248779 · Cited by 1,490
Kuwajima, K. (1989) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340060202 · Cited by 1,439
De Novo Protein Design: Fully Automated Sequence Selection
Dahiyat, B. I., & Mayo, S. L. (1997) · Science · doi:10.1126/science.278.5335.82 · Cited by 1,145
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
Booth, D. R., Sunde, M., Bellotti, V., Robinson, C. V., Hutchinson, W. L., Fraser, P. E., Hawkins, P. N., Dobson, C. M., Radford, S. E., Blake, C. C. F., et al. (1997) · Nature · doi:10.1038/385787a0 · Cited by 1,048
The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
Kelly, J. W. (1998) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(98)80016-x · Cited by 1,001
INGRAM, V. M. (1957) · Nature · doi:10.1038/180326a0 · Cited by 978
Backbone-dependent Rotamer Library for Proteins Application to Side-chain Prediction
Dunbrack, R. L., & Karplus, M. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1170 · Cited by 923
A Third Recognition Element in Bacterial Promoters: DNA Binding by the α Subunit of RNA Polymerase
Ross, W., Gosink, K. K., Salomon, J., Igarashi, K., Zou, C., Ishihama, A., Severinov, K., & Gourse, R. L. (1993) · Science · doi:10.1126/science.8248780 · Cited by 789
Bayesian statistical analysis of protein side‐chain rotamer preferences
Dunbrack, R. L., & Cohen, F. E. (1997) · Protein Science · doi:10.1002/pro.5560060807 · Cited by 774
Protein Design by Binary Patterning of Polar and Nonpolar Amino Acids
Kamtekar, S., Schiffer, J. M., Xiong, H., Babik, J. M., & Hecht, M. H. (1993) · Science · doi:10.1126/science.8259512 · Cited by 730
Lesk, A. M., & Chothia, C. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90373-3 · Cited by 711
Evidence for a molten globule state as a general intermediate in protein folding
Ptitsyn, O. B., Pain, R. H., Semisotnov, G. V., Zerovnik, E., & Razgulyaev, O. I. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80143-7 · Cited by 678
De Novo Design and Structural Characterization of Proteins and Metalloproteins
DeGrado, W. F., Summa, C. M., Pavone, V., Nastri, F., & Lombardi, A. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.779 · Cited by 572
Self-citationDesign and synthesis of multi-haem proteins
Robertson, D. E., Farid, R. S., Moser, C. C., Urbauer, J. L., Mulholland, S. E., Pidikiti, R., Lear, J. D., Wand, A. J., DeGrado, W. F., & Dutton, P. L. (1994) · Nature · doi:10.1038/368425a0 · Cited by 571
Self-citationProtein Design: A Hierarchic Approach
Bryson, J. W., Betz, S. F., Lu, H. S., Suich, D. J., Zhou, H. X., O'Neil, K. T., & DeGrado, W. F. (1995) · Science · doi:10.1126/science.270.5238.935 · Cited by 530
Self-citationStructural Evidence for Induced Fit as a Mechanism for Antibody-Antigen Recognition
Rini, J. M., Schulze-Gahmen, U., & Wilson, I. A. (1992) · Science · doi:10.1126/science.1546293 · Cited by 527
Toward an outline of the topography of a realistic protein-folding funnel.
Onuchic, J. N., Wolynes, P. G., Luthey-Schulten, Z., & Socci, N. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.8.3626 · Cited by 523
Creighton, T. E. (1990) · Biochemical Journal · doi:10.1042/bj2700001 · Cited by 515
Fersht, A. R. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.24.10869 · Cited by 468
McGregor, M. J., Islam, S. A., & Sternberg, M. J. E. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90314-7 · Cited by 420
NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain
Huang, B., Eberstadt, M., Olejniczak, E. T., Meadows, R. P., & Fesik, S. W. (1996) · Nature · doi:10.1038/384638a0 · Cited by 385
Rational design of potent human transthyretin amyloid disease inhibitors.
Sacchettini, J. C., Klabunde, T., Petrassi, H. M., Oza, V. B., Raman, P., & Kelly, J. W. (2000) · Nature Structural Biology · doi:10.1038/74082 · Cited by 379
Conformational analysis of the backbone-dependent rotamer preferences of protein sidechains
Dunbrack, R. L., & Karplus, M. (1994) · Nature Structural & Molecular Biology · doi:10.1038/nsb0594-334 · Cited by 345
Gouda, H., Torigoe, H., Saito, A., Sato, M., Arata, Y., & Shimada, I. (1992) · Biochemistry · doi:10.1021/bi00155a020 · Cited by 341
Design of a 20-Amino Acid, Three-Stranded β-Sheet Protein
Kortemme, T., Ramı́rez-Alvarado, M., & Serrano, L. (1998) · Science · doi:10.1126/science.281.5374.253 · Cited by 324
Design of a Monomeric 23-Residue Polypeptide with Defined Tertiary Structure
Struthers, M. D., Cheng, R. P., & Imperiali, B. (1996) · Science · doi:10.1126/science.271.5247.342 · Cited by 300
Structure of the ColE1 Rop protein at 1.7 Å resolution
Banner, D. W., Kokkinidis, M., & Tsernoglou, D. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90039-8 · Cited by 297
Studies on Protein Stability With T4 Lysozyme
MATTHEWS, B. (1995) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60337-x · Cited by 294
Ho, S. P., & DeGrado, W. F. (1987) · Journal of the American Chemical Society · doi:10.1021/ja00256a032 · Cited by 286
Self-citationFree Energy Balance in Protein Folding
(1995) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60331-9 · Cited by 275
De novo proteins from designed combinatorial libraries
Hecht, M. H., Das, A., Go, A., Bradley, L. H., & Wei, Y. (2004) · Protein Science · doi:10.1110/ps.04690804 · Cited by 268
Solution structure of the tetrameric minimum transforming domain of p53
Lee, W., Harvey, T. S., Yin, Y., Yau, P., Litchfield, D., & Arrowsmith, C. H. (1994) · Nature Structural & Molecular Biology · doi:10.1038/nsb1294-877 · Cited by 265
Design of a heme-binding four-helix bundle
Choma, C. T., Lear, J. D., Nelson, M. J., Dutton, P. L., Robertson, D. E., & DeGrado, W. F. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00082a005 · Cited by 260
Self-citationMetal Ion-Dependent Modulation of the Dynamics of a Designed Protein
Handel, T. M., Williams, S. A., & DeGrado, W. F. (1993) · Science · doi:10.1126/science.8346440 · Cited by 252
Self-citationProbing the role of packing specificity in protein design
Dahiyat, B. I., & Mayo, S. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.19.10172 · Cited by 251
Xu, J., Baase, W. A., Baldwin, E., & Matthews, B. W. (1998) · Protein Science · doi:10.1002/pro.5560070117 · Cited by 229
Schrauber, H., Eisenhaber, F., & Argos, P. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1172 · Cited by 223
Solution structure and dynamics of a de novo designed three-helix bundle protein
Walsh, S. T. R., Cheng, H., Bryson, J. W., Roder, H., & DeGrado, W. F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.10.5486 · Cited by 220
Self-citationLombardi, A., Summa, C. M., Geremia, S., Randaccio, L., Pavone, V., & DeGrado, W. F. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.12.6298 · Cited by 219
Self-citationThe role of internal packing interactions in determining the structure and stability of a protein
Lim, W. A., & Sauer, R. T. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90570-v · Cited by 204
Ferredoxin and ferredoxin–heme maquettes
Gibney, B. R., Mulholland, S. E., Rabanal, F., & Dutton, P. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.26.15041 · Cited by 193
A tetrahedral zinc(II)-binding site introduced into a designed protein
Regan, L., & Clarke, N. D. (1990) · Biochemistry · doi:10.1021/bi00501a003 · Cited by 190
Street, A. G., & Mayo, S. L. (1999) · Structure · doi:10.1016/s0969-2126(99)80062-8 · Cited by 186
Schenck, H. L., & Gellman, S. H. (1998) · Journal of the American Chemical Society · doi:10.1021/ja973984+ · Cited by 185
The de novo design of protein structures
Richardson, J. S., & Richardson, D. C. (1989) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(89)90070-4 · Cited by 184
Three-dimensional structure of the E. coli DMA-binding protein FIS
Kostrewa, D., Granzin, J., Koch, C., Choe, H.-W., Raghunathan, S., Wolf, W., Labahn, J., Kahmann, R., & Saenger, W. (1991) · Nature · doi:10.1038/349178a0 · Cited by 172
Structural and energetic consequences of disruptive mutations in a protein core
Lim, W. A., Farruggio, D. C., & Sauer, R. T. (1992) · Biochemistry · doi:10.1021/bi00132a025 · Cited by 165
Mad Cows Meet Psi-chotic Yeast: The Expansion of the Prion Hypothesis
Lindquist, S. (1997) · Cell · doi:10.1016/s0092-8674(00)80231-7 · Cited by 159
Sequence space, folding and protein design
Cordes, M. H. J., Davidson, A. R., & Sauer, R. T. (1996) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(96)80088-1 · Cited by 154
De novo protein design: from molten globules to native-like states
Betz, S. F., Raleigh, D. P., & DeGrado, W. F. (1993) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(93)90090-8 · Cited by 146
Self-citationAssembly of a Ribonucleoprotein Catalyst by Tertiary Structure Capture
Weeks, K. M., & Cech, T. R. (1996) · Science · doi:10.1126/science.271.5247.345 · Cited by 142
Solution Structure of α2D, a Nativelike de Novo Designed Protein
Hill, R. B., & DeGrado, W. F. (1998) · Journal of the American Chemical Society · doi:10.1021/ja9733649 · Cited by 139
Self-citationGassner, N. C., Baase, W. A., & Matthews, B. W. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12155 · Cited by 138
Geometry of a Black Hole Collision
Matzner, R. A., Seidel, H. E., Shapiro, S. L., Smarr, L. L., Suen, W.-M., Teukolsky, S. A., & Winicour, J. (1995) · Science · doi:10.1126/science.270.5238.941 · Cited by 135
Probing the Determinants of Protein Folding and Stability with Amino Acid Substitutions
Shortle, D. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83544-x · Cited by 132
A designed four helix bundle protein with native-like structure
Schafmeister, C. E., LaPorte, S. L., Miercke, L. J. W., & Stroud, R. M. (1997) · Nature Structural Biology · doi:10.1038/nsb1297-1039 · Cited by 125
Cooperative Interaction between the Three Strands of a Designed Antiparallel β-Sheet
Sharman, G. J., & Searle, M. S. (1998) · Journal of the American Chemical Society · doi:10.1021/ja9705405 · Cited by 124
The hydrophobic-staple motif and a role for loop-residues in α-helix stability and protein folding
Muñoz, V., Blanco, F. J., & Serrano, L. (1995) · Nature Structural & Molecular Biology · doi:10.1038/nsb0595-380 · Cited by 122
Fast events in protein folding
Eaton, W. A., Thompson, P. A., Chan, C.-K., Hage, S. J., & Hofrichter, J. (1996) · Structure · doi:10.1016/s0969-2126(96)00121-9 · Cited by 117
Active barnase variants with completely random hydrophobic cores.
Axe, D. D., Foster, N. W., & Fersht, A. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.11.5590 · Cited by 115
The University of North Carolina at Chapel Hill University Libraries (2020) · PubMed Central · doi:10.17615/jexx-fx48 · Cited by 115
Betz, S. F., & DeGrado, W. F. (1996) · Biochemistry · doi:10.1021/bi960095a · Cited by 110
Self-citationSolution structure of the N-terminal domain of the δ subunit of the E. coli ATPsynthase
Wilkens, S., Dunn, S. D., Chandler, J., Dahlquist, F. W., & Capaldi, R. (1997) · Nature Structural Biology · doi:10.1038/nsb0397-198 · Cited by 108
The crystal structure of a mutant protein with altered but improved hydrophobic core packing.
Lim, W. A., Hodel, A. E., Sauer, R. T., & Richards, F. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.1.423 · Cited by 108
Mirny, L. A., Abkevich, V., & Shakhnovich, E. I. (1996) · Folding and Design · doi:10.1016/s1359-0278(96)00019-3 · Cited by 106
A de Novo Designed Protein Mimics the Native State of Natural Proteins
Raleigh, D. P., Betz, S. F., & DeGrado, W. F. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00133a035 · Cited by 105
Self-citationDe Novo Design of a Novel Heterodinuclear Three‐Helix Bundle Metalloprotein
Ghadiri, M. R., & Case, M. A. (1993) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199315941 · Cited by 102
Dominance in Fishes: The Relation Between Environment and Abundance
Skud, B. E. (1982) · Science · doi:10.1126/science.216.4542.144 · Cited by 99
Amino-acid substitutions in a surface turn modulate protein stability
Predki, P. F., Agrawal, V., Brünger, A. T., & Regan, L. (1996) · Nature Structural Biology · doi:10.1038/nsb0196-54 · Cited by 99
Solution structure and dynamics of a designed hydrophobic core variant of ubiquitin
Johnson, E. C., Lazar, G. A., Desjarlais, J. R., & Handel, T. M. (1999) · Structure · doi:10.1016/s0969-2126(99)80123-3 · Cited by 88
A recipe for designing water‐soluble, β‐sheet‐forming peptides
Mayo, K. H., Ilyina, E. E., & Park, H. (1996) · Protein Science · doi:10.1002/pro.5560050709 · Cited by 81
Design of a Unique Protein Scaffold for Maquettes
Gibney, B. R., Rabanal, F., Skalicky, J. J., Wand, A. J., & Dutton, P. L. (1997) · Journal of the American Chemical Society · doi:10.1021/ja963561s · Cited by 79
Raleigh, D. P., & DeGrado, W. F. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00051a061 · Cited by 79
Self-citationStruthers, M. D., Cheng, R. P., & Imperiali, B. (1996) · Journal of the American Chemical Society · doi:10.1021/ja954014u · Cited by 78
Betz, S. F., Liebman, P. A., & DeGrado, W. F. (1997) · Biochemistry · doi:10.1021/bi961704h · Cited by 77
Self-citationHay, R. W., Hassan, M. M., & You-Quan, C. (1993) · Journal of Inorganic Biochemistry · doi:10.1016/0162-0134(93)85619-j · Cited by 76
Design and NMR analyses of compact, independently folded BBA motifs
Struthers, M. D., Ottesen, J. J., & Imperiali, B. (1998) · Folding and Design · doi:10.1016/s1359-0278(98)00015-7 · Cited by 76
The construction of metal centers in proteins by rational design
Hellinga, H. W. (1998) · Folding and Design · doi:10.1016/s1359-0278(98)00001-7 · Cited by 75
In vitro evolution of thermodynamically stable turns
Zhou, H. X., Hoess, R. H., & DeGrado, W. F. (1996) · Nature Structural Biology · doi:10.1038/nsb0596-446 · Cited by 73
Self-citationLazaridis, T., Tobias, D. J., Brooks, C. L., & Paulaitis, M. E. (1991) · The Journal of Chemical Physics · doi:10.1063/1.461335 · Cited by 68
Tertiary templates for the design of diiron proteins
Summa, C. M., Lombardi, A., Lewis, M., & DeGrado, W. F. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)80071-2 · Cited by 63
Self-citationGlykos, N. M., Cesareni, G., & Kokkinidis, M. (1999) · Structure · doi:10.1016/s0969-2126(99)80081-1 · Cited by 60
Roy, S., & Hecht, M. H. (2000) · Biochemistry · doi:10.1021/bi992328e · Cited by 59
Defining the core structure of the α-lactalbumin molten globule state 1 1Edited by C. R. Matthews
Demarest, S. J., Boice, J. A., Fairman, R., & Raleigh, D. P. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3228 · Cited by 59
Self-citationPatterns of loop regions in proteins
Efimov, A. V. (1993) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(05)80110-1 · Cited by 51
Vogel, E., Dörr, J., Herrmann, A., Lex, J., Schmickler, H., Walgenbach, P., Gisselbrecht, J. P., & Gross, M. (1993) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199315971 · Cited by 50
Pan, C. J., Hoeppner, W., & CHOU, J. Y. (1990) · Biochemistry · doi:10.1021/bi00501a004 · Cited by 49
Solution structure of αtα, a helical hairpin peptide of de novo design
Fezoui, Y., Connolly, P. J., & Osterhout, J. J. (1997) · Protein Science · doi:10.1002/pro.5560060907 · Cited by 48
A polar, solvent-exposed residue can be essential for native protein structure
Hill, R. B., & DeGrado, W. F. (2000) · Structure · doi:10.1016/s0969-2126(00)00130-1 · Cited by 47
Self-citationHydrophobic core packing and protein design
Lazar, G. A., & Handel, T. M. (1998) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(98)80102-6 · Cited by 41
Protein folding from a combinatorial perspective
Sauer, R. T. (1996) · Folding and Design · doi:10.1016/s1359-0278(96)00015-6 · Cited by 40
Histidine placement in de novo–designed heme proteins
Gibney, B. R., & Dutton, P. L. (1999) · Protein Science · doi:10.1110/ps.8.9.1888 · Cited by 38
Gibney, B. R., Rabanal, F., & Dutton, P. L. (1997) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(97)80050-6 · Cited by 37
Design of peptides undergoing self-catalytic α-to-β transition and amyloidogenesis
Mihara, H., Takahashi, Y., & Ueno, A. (1998) · Biopolymers · Cited by 37
The Sal-XH Motif for Metal-Mediated Oxidative DNA−Peptide Cross-Linking
Stemmler, A. J., & Burrows, C. J. (1999) · Journal of the American Chemical Society · doi:10.1021/ja991164m · Cited by 30
Selective Recognition and Cleavage of RNA Loop Structures by Ni(II)·Xaa-Gly-His Metallopeptides
Brittain, I. J., Huang, X., & Long, E. C. (1998) · Biochemistry · doi:10.1021/bi9806605 · Cited by 30
Hydrogen Bonded Cluster Can Specify the Native State of a Protein
Hill, R. B., Hong, J.-K., & DeGrado, W. F. (2000) · Journal of the American Chemical Society · doi:10.1021/ja9919332 · Cited by 23
Self-citation
Cited by
The Design of Coiled-Coil Structures and Assemblies
Woolfson, D. N. (2005) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(05)70004-8 · Cited by 585
Principles for designing ideal protein structures
Koga, N., Tatsumi-Koga, R., Liu, G., Xiao, R., Acton, T. B., Montelione, G. T., & Baker, D. (2012) · Nature · doi:10.1038/nature11600 · Cited by 564
Protein Design: Toward Functional Metalloenzymes
Yu, F., Cangelosi, V. M., Zastrow, M. L., Tegoni, M., Plegaria, J. S., Tebo, A. G., Mocny, C. S., Ruckthong, L., Qayyum, H., & Pecoraro, V. L. (2014) · Chemical Reviews · doi:10.1021/cr400458x · Cited by 441
Protein Design: From the Aspect of Water Solubility and Stability
Qing, R., Hao, S., Smorodina, E., Jin, D., Zalevsky, A., & Zhang, S. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00757 · Cited by 312
High thermodynamic stability of parametrically designed helical bundles
Huang, P.-S., Oberdorfer, G., Xu, C., Pei, X. Y., Nannenga, B. L., Rogers, J. M., DiMaio, F., Gonen, T., Luisi, B., & Baker, D. (2014) · Science · doi:10.1126/science.1257481 · Cited by 277
Metadata
- Authors
- Hill, R. B., Raleigh, D. P., Lombardi, A., & DeGrado, W. F.
- Venue
- Accounts of Chemical Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2000-10-24
- Volume
- 33
- Issue
- 11
- Pages
- 745-754
- ISSN
- 0001-4842 (ISSN-L)
- 1520-4898
- OpenAlex
- W2090265120
- Cited by
- 300
- References
- 104
- FWCI
- 4.84
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
