Cited by 401Computational Drug Discovery MethodsChemical Synthesis and AnalysisEnzyme Structure and Function

The DOI matches its Crossref record; 78 of the 78 references it cites were found in a registry or an index.

Tethering: Fragment-Based Drug Discovery

Erlanson, Daniel A., Wells, James A., Braisted, Andrew C.·2004·Annual Review of Biophysics and Biomolecular Structure

DOI 10.1146/annurev.biophys.33.110502.140409

Open this paper in CoChat — free account

Abstract

▪ Abstract The genomics revolution has provided a deluge of new targets for drug discovery. To facilitate the drug discovery process, many researchers are turning to fragment-based approaches to find lead molecules more efficiently. One such method, Tethering 1 , allows for the identification of small-molecule fragments that bind to specific regions of a protein target. These fragments can then be elaborated, combined with other molecules, or combined with one another to provide high-affinity drug leads. In this review we describe the background and theory behind Tethering and discuss its use in identifying novel inhibitors for protein targets including interleukin-2 (IL-2), thymidylate synthase (TS), protein tyrosine phosphatase 1B (PTP-1B), and caspases.

Integrity signals

Registry

Crossref · 10.1146/annurev.biophys.33.110502.140409

Cites

78 of 78 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

A Combinatorial Approach Defines Specificities of Members of the Caspase Family and Granzyme B
Thornberry, N. A., Rano, T. A., Peterson, E. P., Rasper, D., Timkey, T., Garcia-Calvo, M. M., Houtzager, V. M., Nordstrom, P. A., Roy, S., Vaillancourt, J. P., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.29.17907 · Cited by 2,089
Discovering High-Affinity Ligands for Proteins: SAR by NMR
Shuker, S. B., Hajduk, P. J., Meadows, R. P., & Fesik, S. W. (1996) · Science · doi:10.1126/science.274.5292.1531 · Cited by 2,045
Structural Mechanism for STI-571 Inhibition of Abelson Tyrosine Kinase
Schindler, T. H., Bornmann, W. G., Pellicena, P., Miller, W. T., Clarkson, B., & Kuriyan, J. (2000) · Science · doi:10.1126/science.289.5486.1938 · Cited by 1,785
The Conformational Plasticity of Protein Kinases
Huse, M., & Kuriyan, J. (2002) · Cell · doi:10.1016/s0092-8674(02)00741-9 · Cited by 1,760
Irreversible Inhibitors of Serine, Cysteine, and Threonine Proteases
Powers, J. C., Asgian, J. L., Ekici, Ö. D., & James, K. E. (2002) · Chemical Reviews · doi:10.1021/cr010182v · Cited by 1,090 · cited 1×
“These include proteases (27, 29, 30, 57, 59, 63), kinases (24, 74), and phosphatases (4, 28, 50), all classes of enzymes that are heavily pursued in the pharmaceutical industry.”
Background
A Common Mechanism Underlying Promiscuous Inhibitors from Virtual and High-Throughput Screening
McGovern, S. L., Caselli, E., Grigorieff, N., & Shoichet, B. K. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm010533y · Cited by 1,048
Inhibition of Human Caspases by Peptide-based and Macromolecular Inhibitors
Garcia-Calvo, M. M., Peterson, E. P., Leiting, B., Ruel, R., Nicholson, D. W., & Thornberry, N. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.49.32608 · Cited by 980
On the attribution and additivity of binding energies
Jencks, W. P. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.7.4046 · Cited by 938
Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site
Pargellis, C., Tong, L., Churchill, L., Cirillo, P. F., Gilmore, T., Graham, A. G., Grob, P. M., Hickey, E. R., Moss, N., Pav, S., et al. (2002) · Nature Structural Biology · doi:10.1038/nsb770 · Cited by 834
Unraveling hot spots in binding interfaces: progress and challenges
DeLano, W. L. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00283-x · Cited by 767
Cysteine Proteases and Their Inhibitors
Otto, H., & Schirmeister, T. (1997) · Chemical Reviews · doi:10.1021/cr950025u · Cited by 760
Protein tyrosine phosphatase 1B inhibitors for diabetes
Johnson, T., Ermolieff, J., & Jirousek, M. R. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd895 · Cited by 660
[2] Thiol/disulfide exchange equilibria and disulfidebond stability
Gilbert, H. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)51107-5 · Cited by 549
High-throughput crystallography for lead discovery in drug design
Blundell, T. L., Jhoti, H., & Abell, C. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd706 · Cited by 538
Drug discovery by dynamic combinatorial libraries
Ramström, O., & Lehn, J. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd704 · Cited by 510
Regulation of PTP1B via Glutathionylation of the Active Site Cysteine 215
Barrett, W. C., DeGnore, J. P., König, S., Fales, H. M., Keng, Y., Zhang, Z., Yim, M. B., & Chock, P. B. (1999) · Biochemistry · doi:10.1021/bi990240v · Cited by 488
Biology of the Interleukin-2 Receptor
Nelson, B. H., & Willerford, D. M. (1998) · Advances in immunology · doi:10.1016/s0065-2776(08)60386-7 · Cited by 475
Preferential Heterodimer Formation by Isolated Leucine Zippers from Fos and Jun
O’Shea, E. K., Rutkowski, R., Stafford, W. F., & Kim, P. S. (1989) · Science · doi:10.1126/science.2503872 · Cited by 471
Molecular Basis for the Dephosphorylation of the Activation Segment of the Insulin Receptor by Protein Tyrosine Phosphatase 1B
Salmeen, A. E., Andersen, J. N., Myers, M. P., Tonks, N. K., & Barford, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00137-4 · Cited by 470
Site-directed ligand discovery
Erlanson, D. A., Braisted, A. C., Raphael, D. R., Randal, M., Stroud, R. M., Gordon, E. M., & Wells, J. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.17.9367 · Cited by 466
Self-citation
Virtual combinatorial libraries: Dynamic generation of molecular and supramolecular diversity by self-assembly
Huc, I., & Lehn, J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2106 · Cited by 461
Protein Tyrosine Phosphatases: Structure and Function, Substrate Specificity, and Inhibitor Development
Zhang, Z. (2002) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.42.083001.144616 · Cited by 435
Specific, irreversible inactivation of the epidermal growth factor receptor and erbB2, by a new class of tyrosine kinase inhibitor
Fry, D. W., Bridges, A. J., Denny, W. A., Doherty, A. M., Greis, K. D., Hicks, J. L., Hook, K. E., Keller, P. R., Leopold, W. R., Loo, J. A., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.12022 · Cited by 424
Dynamic Combinatorial Chemistry
Lehn, J., & Eliseev, A. V. (2001) · Science · doi:10.1126/science.1060066 · Cited by 403
Nonleadlikeness and leadlikeness in biochemical screening
Rishton, G. M. (2003) · Drug Discovery Today · doi:10.1016/s1359644602025722 · Cited by 381
Novel Inhibitors of DNA Gyrase: 3D Structure Based Biased Needle Screening, Hit Validation by Biophysical Methods, and 3D Guided Optimization. A Promising Alternative to Random Screening
Boehm, H.-J., Boehringer, M., Bur, D., Gmuender, H., Huber, W., Klaus, W., Kostrewa, D., Kuehne, H., Luebbers, T., Meunier-Keller, N., et al. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm000017s · Cited by 376
Binding of small molecules to an adaptive protein–protein interface
Arkin, M. R., Randal, M., DeLano, W. L., Hyde, J., Luong, T. N., Oslob, J. D., Raphael, D. R., Taylor, L., Wang, J., McDowell, R. S., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252756299 · Cited by 376
Self-citation
Discovering novel ligands for macromolecules using X-ray crystallographic screening
Nienaber, V. L., Richardson, P. L., Klighofer, V., Bouska, J. J., Giranda, V. L., & Greer, J. (2000) · Nature Biotechnology · doi:10.1038/80319 · Cited by 322
Inhibition of Protein−Protein Association by Small Molecules: Approaches and Progress
Toogood, P. L. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm010468s · Cited by 281
The SHAPES strategy: an NMR-based approach for lead generation in drug discovery
Fejzo, J., Lepre, C. A., Peng, J. W., Bemis, G. W., Ajay, Murcko, M. A., & Moore, J. M. (1999) · Chemistry & Biology · doi:10.1016/s1074-5521(00)80022-8 · Cited by 279
6-Substituted-4-(3-bromophenylamino)quinazolines as Putative Irreversible Inhibitors of the Epidermal Growth Factor Receptor (EGFR) and Human Epidermal Growth Factor Receptor (HER-2) Tyrosine Kinases with Enhanced Antitumor Activity
Tsou, H., Mamuya, N. N., Johnson, B. D., Reich, M. F., Gruber, B. C., Ye, F., Nilakantan, R., Shen, R., Discafani, C. M., DeBlanc, R., et al. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm0005555 · Cited by 269
Discovery of a Potent Small Molecule IL-2 Inhibitor through Fragment Assembly
Braisted, A. C., Oslob, J. D., DeLano, W. L., Hyde, J., McDowell, R. S., Waal, N. D., Yu, C. H., Arkin, M. R., & Raimundo, B. C. (2003) · Journal of the American Chemical Society · doi:10.1021/ja034247i · Cited by 256
Self-citation
Substrate and Inhibitor Specificity of Interleukin-1β-converting Enzyme and Related Caspases
Margolin, N., Raybuck, S. A., Wilson, K. P., Chen, W., Fox, T., Gu, Y., & Livingston, D. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.11.7223 · Cited by 244
Structure-reactivity relations for thiol-disulfide interchange
Houk, J., & Whitesides, G. M. (1987) · Journal of the American Chemical Society · doi:10.1021/ja00256a040 · Cited by 238
In situ assembly of enzyme inhibitors using extended tethering
Erlanson, D. A., Lam, J. W., Wiesmann, C., Luong, T. N., Simmons, R. L., DeLano, W. L., Choong, I., Burdett, M. T., Flanagan, W. M., Lee, D. M., et al. (2003) · Nature Biotechnology · doi:10.1038/nbt786 · Cited by 204
Self-citation
SAR by MS: A Ligand Based Technique for Drug Lead Discovery Against Structured RNA Targets
Swayze, E. E., Jefferson, E. A., Sannes, K. A., Blyn, L. B., Risen, L. M., Arakawa, S., Osgood, S. A., Hofstadler, S. A., & Griffey, R. H. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm0255466 · Cited by 145
P1 Aspartate-Based Peptide .alpha.-((2,6-Dichlorobenzoyl)oxy)methyl Ketones as Potent Time-Dependent Inhibitors of Interleukin-1.beta.-Converting Enzyme
Dolle, R. E., Hoyer, D., Prasad, C. V. C., Schmidt, S. J., Helaszek, C. T., Miller, R. E., & Ator, M. A. (1994) · Journal of Medicinal Chemistry · doi:10.1021/jm00031a003 · Cited by 143
A Minimal Peptide Scaffold for β-Turn Display: Optimizing a Strand Position in Disulfide-Cyclized β-Hairpins
Cochran, A. G., Tong, R. T., Starovasnik, M. A., Park, E. J., McDowell, R. S., Theaker, J., & Skelton, N. J. (2000) · Journal of the American Chemical Society · doi:10.1021/ja003369x · Cited by 136
Discovery and SAR of a Novel Selective and Orally Bioavailable Nonpeptide Classical Competitive Inhibitor Class of Protein-Tyrosine Phosphatase 1B
Andersen, H. S., Olsen, O. H., Iversen, L. F., Sørensen, A. L. P., Mortensen, S. B., Christensen, M. S., Branner, S., Hansen, T. K., Lau, J. F., Jeppesen, L., et al. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm0209026 · Cited by 135
Kinetics and equilibria of thiol/disulfide interchange reactions of selected biological thiols and related molecules with oxidized glutathione
Keire, D. A., Strauss, E. J., Guo, W., Noszál, B., & Rabenstein, D. L. (1992) · The Journal of Organic Chemistry · doi:10.1021/jo00027a023 · Cited by 134
Protein–protein interfaces: mimics and inhibitors
Cochran, A. G. (2001) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(01)00262-9 · Cited by 133
Identification of a Small Molecule Inhibitor of the IL-2/IL-2Rα Receptor Interaction Which Binds to IL-2
Tilley, J., Chen, L., Fry, D. C., Emerson, S. D., Powers, G. D., Biondi, D. A., Varnell, T. A., Trilles, R. V., Guthrie, R. W., Mennona, F. A., et al. (1997) · Journal of the American Chemical Society · doi:10.1021/ja970702x · Cited by 129
α-Haloacetophenone Derivatives As Photoreversible Covalent Inhibitors of Protein Tyrosine Phosphatases
Arabacı, G., Guo, X., Beebe, K. D., Coggeshall, K. M., & Pei, D. (1999) · Journal of the American Chemical Society · doi:10.1021/ja9906756 · Cited by 124
Structural Basis of Plasticity in Protein Tyrosine Phosphatase 1B Substrate Recognition,
Sarmiento, M., Puius, Y. A., Vetter, S. W., Keng, Y., Wu, L., Zhao, Y. C., Lawrence, D. S., Almo, S. C., & Zhang, Z. (2000) · Biochemistry · doi:10.1021/bi000319w · Cited by 119
Identification of Potent and Selective Small-Molecule Inhibitors of Caspase-3 through the Use of Extended Tethering and Structure-Based Drug Design
Choong, I., Lew, W., Lee, D. M., Pham, P., Burdett, M. T., Lam, J. W., Wiesmann, C., Luong, T. N., Fahr, B. J., DeLano, W. L., et al. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm020230j · Cited by 106
Self-citation
Potent Small-Molecule Binding to a Dynamic Hot Spot on IL-2
Thanos, C. D., Randal, M., & Wells, J. A. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0382617 · Cited by 105
Self-citation
Mode of interaction of .beta.-hydroxy-.beta.-methylglutaryl coenzyme A reductase with strong binding inhibitors: compactin and related compounds
Nakamura, C. E., & Abeles, R. H. (1985) · Biochemistry · doi:10.1021/bi00327a014 · Cited by 105
Localization in human interleukin 2 of the binding site to the alpha chain (p55) of the interleukin 2 receptor.
Sauvé, K., Nachman-Clewner, M., Spence, C. L., Bailon, P., Campbell, E., Tsien, W. H., Kondas, J. A., Hakimi, J., & Ju, G. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.11.4636 · Cited by 100
Affinity Selection and Mass Spectrometry-Based Strategies to Identify Lead Compounds in Combinatorial Libraries
Kaur, S., McGuire, L., Tang, D., Dollinger, G., & Huebner, V. (1997) · Journal of Protein Chemistry · doi:10.1023/a:1026369729393 · Cited by 95
SAR and X-ray. A New Approach Combining Fragment-Based Screening and Rational Drug Design: Application to the Discovery of Nanomolar Inhibitors of Src SH2
Lesuisse, D., Lange, G., Deprez, P., Bénard, D., Schoot, B. M., Delettre, G., Marquette, J.-P., Broto, P., Jean‐Baptiste, V., Bichet, P., et al. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm010927p · Cited by 90
Phosphoryltyrosyl mimetics in the design of peptide-based signal transduction inhibitors
Burke, T. R., Yao, Z., Liu, D., Voigt, J. H., & Gao, Y. (2001) · Biopolymers · doi:10.1002/1097-0282(2001)60:1 · Cited by 87
Definition and spatial location of mouse interleukin‐2 residues that interact with its heterotrimeric receptor.
Zurawski, S., Vega, F., Doyle, E. L., Huyghe, B. G., Flaherty, K. M., McKay, D., & Zurawski, G. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06206.x · Cited by 82
Mechanism-Based Inactivation of Prostatic Acid Phosphatase
Myers, J. K., & Widlanski, T. S. (1993) · Science · doi:10.1126/science.8248785 · Cited by 78
The additivity of substrate fragments in enzyme–ligand binding
Stout, T. J., Sage, C. R., & Stroud, R. M. (1998) · Structure · doi:10.1016/s0969-2126(98)00086-0 · Cited by 77
Recent advances in the synthesis, design and selection of cysteine protease inhibitors
Hernández, A. Á., & Roush, W. R. (2002) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(02)00345-9 · Cited by 72
Structure-based screening and design in drug discovery
van Dongen, M. J. P., Weigelt, J., Uppenberg, J., Schultz, J., & Wikström, M. (2002) · Drug Discovery Today · doi:10.1016/s1359-6446(02)02233-x · Cited by 71
Use of Strain in a Stereospecific Catalytic Mechanism: Crystal Structures of Escherichia coli Thymidylate Synthase Bound to FdUMP and Methylenetetrahydrofolate,
Hyatt, D. C., Maley, F., & Montfort, W. R. (1997) · Biochemistry · doi:10.1021/bi962936j · Cited by 68
Second-Site NMR Screening and Linker Design
Jahnke, W., Flörsheimer, A., Blommers, M. J. J., PARIS, C. G., Heim, J., Nalin, C. M., & Perez, L. B. (2003) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026033392778 · Cited by 66
Discovery and Structure−Activity Relationship of Oxalylarylaminobenzoic Acids as Inhibitors of Protein Tyrosine Phosphatase 1B
Liu, G., Szczepankiewicz, B. G., Pei, Z., Janowick, D. A., Xin, Z., Hajduk, P. J., Abad‐Zapatero, C., Liang, H., Hutchins, C. W., Fesik, S. W., et al. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm0205696 · Cited by 64
Application of NMR Screening in Drug Discovery
Fejzo, J., Lepre, C. A., & Xie, X. (2003) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026033392796 · Cited by 56
Structural basis for recognition of polyglutamyl folates by thymidylate synthase
Kamb, A., Finer-Moore, J. S., Calvert, H., & Stroud, R. M. (1992) · Biochemistry · doi:10.1021/bi00156a005 · Cited by 54
Peptide Library Approach with a Disulfide Tether to Refine the Tom20 Recognition Motif in Mitochondrial Presequences
Obita, T., Muto, T., Endo, T., & Kohda, D. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00288-2 · Cited by 53
Discovery and Characterization of Cooperative Ligand Binding in the Adaptive Region of Interleukin-2
Hyde, J., Braisted, A. C., Randal, M., & Arkin, M. R. (2003) · Biochemistry · doi:10.1021/bi034138g · Cited by 49
Self-citation
Discovery of a New Phosphotyrosine Mimetic for PTP1B Using Breakaway Tethering
Erlanson, D. A., McDowell, R. S., He, M. M., Randal, M., Simmons, R. L., Kung, J., Waight, A. B., & Hansen, S. K. (2003) · Journal of the American Chemical Society · doi:10.1021/ja034440c · Cited by 48
Self-citation
Structure-Based Screening As Applied to Human FABP4: A Highly Efficient Alternative to HTS for Hit Generation
van Dongen, M. J. P., Uppenberg, J., Svensson, S., Lundbäck, T., Åkerud, T., Wikström, M., & Schultz, J. (2002) · Journal of the American Chemical Society · doi:10.1021/ja017830c · Cited by 48
Design and Synthesis of Potent Non-Polyglutamatable Quinazoline Antifolate Thymidylate Synthase Inhibitors
Marsham, P. R., Wardleworth, J. M., Boyle, F. T., Hennequin, L. F., Kimbell, R., Brown, M., & Jackman, A. L. (1999) · Journal of Medicinal Chemistry · doi:10.1021/jm9803727 · Cited by 46
Design of Small Molecule Libraries for NMR Screening and Other Applications in Drug Discovery
Jacoby, E., Davies, J. W., & Blommers, M. J. J. (2002) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026033392606 · Cited by 44
Apoptosis: a potential target for discovering novel therapies for cardiovascular diseases
Yue, T., Ohlstein, E. H., & Ruffolo, R. R., Jr. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)80069-6 · Cited by 43
Structure-based studies on species-specific inhibition of thymidylate synthase
Costi, M. P., Tondi, D., Rinaldi, M., Barlocco, D., Pecorari, P., Soragni, F., Venturelli, A., & Stroud, R. M. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(02)00083-2 · Cited by 37
Deconstruction of GCN4/GCRE into a monomeric peptide-DNA complex
Stanojević, D., & Verdine, G. (1995) · Nature Structural Biology · doi:10.1038/nsb0695-450 · Cited by 34
In vitro characterization of nonpeptide irreversible inhibitors of HIV proteases.
Salto, R., Babé, L. M., Li, J., Rose, J., Yu, Z., Burlingame, A. L., Voss, J. J. D., SUI, Z., de Montellano, P. R. O., & Craik, C. S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34114-5 · Cited by 32
Design and Synthesis of Non-peptidic Inhibitors for the Syk C-Terminal SH2 Domain Based on Structure-Based In-Silico Screening
Niimi, T., Orita, M., Okazawa-Igarashi, M., Sakashita, H., Kikuchi, K., Ball, E., Ichikawa, A., Yamagiwa, Y., Sakamoto, S., Tanaka, A., et al. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm010313k · Cited by 29
Identification of potent and novel small-Molecule inhibitors of caspase-3
Allen, D. A., Pham, P., Choong, I., Fahr, B. J., Burdett, M. T., Lew, W., DeLano, W. L., Gordon, E. M., Lam, J. W., O'Brien, T., et al. (2003) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2003.08.024 · Cited by 27
Selective inactivation of protein tyrosine phosphatase PTP1B by sulfone analogue of naphthoquinone
Ham, S. W., Park, J., Lee, S., & Yoo, J. S. (1999) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(98)00725-2 · Cited by 14
Caspase inhibitors - A chemist's perspective.
Graczyk, P. P. (1999) · PubMed · Cited by 13
Emerging therapeutic targets in caspase-dependent disease
McBride, C. B., McPhail, L. T., & Steeves, J. D. (1999) · Emerging Therapeutic Targets · doi:10.1517/14728222.3.3.391 · Cited by 13
A Novel Strategy for Designing Irreversible Inhibitors of Metalloproteases: Acetals as Latent Electrophiles That Interact with Catalytic Nucleophile at the Active Site
Han, M. S., Ryu, C. H., Chung, S. J., & Kim, D. H. (2000) · Organic Letters · doi:10.1021/ol006346w · Cited by 7
The art and practice of structure-based drug design: A molecular modeling perspective
(1996) · doi:10.1002/(sici)1098-1128(199601)16:1

Research works printed but not linked: 1

Graczyk PP, 1999, Restor. Neurol. Neurosci., 14, 1

Sorted by citations

A decade of fragment-based drug design: strategic advances and lessons learned
Hajduk, P., & Greer, J. (2007) · Nature reviews. Drug discovery · doi:10.1038/nrd2220 · Cited by 1,004
Small-Molecule Inhibitors of Protein-Protein Interactions: Progressing toward the Reality
Arkin, M. R., Tang, Y., & Wells, J. A. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.09.001 · Cited by 1,065
Self-citation
Navigating chemical space for biology and medicine
Lipinski, C. A., & Hopkins, A. L. (2004) · Nature · doi:10.1038/nature03193 · Cited by 1,028
Advances in covalent drug discovery
Boike, L., Henning, N. J., & Nomura, D. K. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00542-z · Cited by 823
Allosteric regulation and catalysis emerge via a common route
Goodey, N. M., & Benkovic, S. J. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.98 · Cited by 668

See all 401

Authors: Erlanson, D. A., Wells, J. A., & Braisted, A. C.
Affiliations: Sunesis (United States) (US)
ORCID: Erlanson, Daniel A.
Wells, James A.
Venue: Annual Review of Biophysics and Biomolecular Structure
Publisher: Annual Reviews
Published: 2004-06-09
Volume: 33
Issue: 1
Pages: 199-223
ISSN: 1056-8700 (ISSN-L)
1545-4266
DOI: 10.1146/annurev.biophys.33.110502.140409
OpenAlex: W2138958920
Cited by: 385
References: 78
Citations by year: 2026: 5 · 2025: 7 · 2024: 17 · 2023: 16 · 2022: 17 · 2021: 8 · 2020: 17 · 2019: 17 · 2018: 21 · 2017: 6 · 2016: 18 · 2015: 21 · 2014: 23 · 2013: 11 · 2012: 29
FWCI: 1.77
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Biophysics and Biomolecular Structure (publishedVersion)
PubMed (publishedVersion)
Funders: Sunesis
Topics: Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Drug Discovery › Computational Drug Discovery Methods
Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: tethering, fragment-based drug discovery, small-molecule fragments, protein-ligand binding, lead compound identification, interleukin-2, thymidylate synthase, PTP1B, caspases, protein inhibitors
MeSH terms: Binding Sites, Peptide Fragments, Protein Binding, Proteins, Drug Design, Protein Interaction Mapping, Protein Array Analysis

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

Tethering: Fragment-Based Drug Discovery

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks