Cited by 602Protein Kinase Regulation and GTPase SignalingProtein Structure and DynamicsProtein Tyrosine Phosphatases

The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.

Atomic structure of the MAP kinase ERK2 at 2.3 A resolution

Zhang, Faming, Strand, Arne, Robbins, David, Cobb, Melanie H., Goldsmith, Elizabeth J.·1994·Nature

Open this paper in CoChat — free account

Abstract

The structure of the MAP kinase ERK2, a ubiquitous protein kinase target for regulation by Ras and Raf, has been solved in its unphosphorylated low-activity conformation to a resolution of 2.3 A. The two domains of unphosphorylated ERK2 are farther apart than in the active conformation of cAMP-dependent protein kinase and the peptide-binding site is blocked by tyrosine 185, one of the two residues that are phosphorylated in the active enzyme. Activation of ERK2 is thus likely to involve both global and local conformational changes.

Integrity signals

Registry

Crossref · 10.1038/367704a0

Cites

52 of 52 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?

Improved methods for building protein models in electron density maps and the location of errors in these models
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616
The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic Domains
Hanks, S. K., Quinn, A. M., & Hunter, T. R. (1988) · Science · doi:10.1126/science.3291115 · Cited by 5,040
Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery
Perutz, M. F. (1970) · Nature · doi:10.1038/228726a0 · Cited by 2,914
Crystallographic R Factor Refinement by Molecular Dynamics
Brünger, A. T., Kuriyan, J., & Karplus, M. (1987) · Science · doi:10.1126/science.235.4787.458 · Cited by 1,950
ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF
Boulton, T. G., Nye, S. H., Robbins, D. J., Ip, N. Y., Radzlejewska, E., Morgenbesser, S. D., DePinho, R. A., Panayotatos, N., Cobb, M. H., & Yancopoulos, G. D. (1991) · Cell · doi:10.1016/0092-8674(91)90098-j · Cited by 1,876
Self-citation
A graphics model building and refinement system for macromolecules
Jones, T. A. (1978) · Journal of Applied Crystallography · doi:10.1107/s0021889878013308 · Cited by 1,833
Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase
Knighton, D. R., Zheng, J., Eyck, L. F. T., Ashford, V. A., Xuong, N., Taylor, S. S., & Sowadski, J. M. (1991) · Science · doi:10.1126/science.1862342 · Cited by 1,764
Phosphorylation of c-jun mediated by MAP kinases
Pulverer, B., Kyriakis, J. M., Avruch, J., Nikolakaki, E., & Woodgett, J. R. (1991) · Nature · doi:10.1038/353670a0 · Cited by 1,470
MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo.
Sun, H., Charles, C. H., Lau, L. F., & Tonks, N. K. (1993) · Cell · doi:10.1016/0092-8674(93)90383-2 · Cited by 1,156
Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase
Anderson, N. G., Maller, J. L., Tonks, N. K., & Sturgill, T. W. (1990) · Nature · doi:10.1038/343651a0 · Cited by 1,064
Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II
Sturgill, T. W., Ray, L. B., ERIKSON, E., & Maller, J. L. (1988) · Nature · doi:10.1038/334715a0 · Cited by 1,017
Crystal structure of cyclin-dependent kinase 2
Bondt, H. L. D., Rosenblatt, J., Jancarik, J., Jones, H. D., Morgan, D. O., & Kim, S. (1993) · Nature · doi:10.1038/363595a0 · Cited by 990
Complexes of Ras⋅GTP with Raf-1 and Mitogen-Activated Protein Kinase Kinase
Moodie, S. A., Willumsen, B. M., Weber, M. J., & Wolfman, A. (1993) · Science · doi:10.1126/science.8503013 · Cited by 968
Structure of a Peptide Inhibitor Bound to the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase
Knighton, D. R., Zheng, J., Eyck, L. F. T., Xuong, N., Taylor, S. S., & Sowadski, J. M. (1991) · Science · doi:10.1126/science.1862343 · Cited by 960
Phosphorylation of transcription factor p62TCF by MAP kinase stimulates ternary complex formation at c-fos promoter
Gille, H., Sharrocks, A. D., & Shaw, P. E. (1992) · Nature · doi:10.1038/358414a0 · Cited by 946
The Primary Structure of MEK, a Protein Kinase that Phosphorylates the ERK Gene Product
Crews, C. M., Alessandrini, A., & Erikson, R. L. (1992) · Science · doi:10.1126/science.1411546 · Cited by 930
A Divergence in the MAP Kinase Regulatory Network Defined by MEK Kinase and Raf
Lange-Carter, C. A., Pleiman, C. M., Gardner, A. M., Blumer, K. J., & Johnson, G. L. (1993) · Science · doi:10.1126/science.8385802 · Cited by 827
An Insulin-Stimulated Protein Kinase Similar to Yeast Kinases Involved in Cell Cycle Control
Boulton, T. G., Yancopoulos, G. D., Gregory, J. S., Slaughter, C. A., Moomaw, C. R., Hsu, J., & Cobb, M. H. (1990) · Science · doi:10.1126/science.2164259 · Cited by 707
Self-citation
Rapid stimulation by insulin of a serine/threonine kinase in 3T3-L1 adipocytes that phosphorylates microtubule-associated protein 2 in vitro.
Ray, L. B., & Sturgill, T. W. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.6.1502 · Cited by 592
Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer‐like state.
Drewes, G., Lichtenberg‐Kraag, B., Döring, F., Mandelkow, E. M., Biernat, J., Goris, J., Dorée, M., & Mandelkow, E. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05272.x · Cited by 565
Ribbon models of macromolecules
Carson, M. (1987) · Journal of Molecular Graphics · doi:10.1016/0263-7855(87)80010-3 · Cited by 514
The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation
Sontag, E., Fedorov, S. A., Kamibayashi, C., Robbins, D. J., Cobb, M. H., & Mumby, M. C. (1993) · Cell · doi:10.1016/0092-8674(93)90533-v · Cited by 510
Self-citation
Regulation and properties of extracellular signal-regulated protein kinases 1 and 2 in vitro.
Robbins, D. J., Zhen, E., Owaki, H., Vanderbilt, C. A., Ebert, D. J., Geppert, T. D., & Cobb, M. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53507-9 · Cited by 499
Self-citation
Multiple components in an epidermal growth factor-stimulated protein kinase cascade
Ahn, N. G., Seger, R., Bratlien, R. L., Diltz, C. D., Tonks, N. K., & Krebs, E. G. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64310-1 · Cited by 492
Extracellular signal-regulated kinases: ERKs in progress.
Cobb, M. H., Boulton, T. G., & Robbins, D. J. (1991) · Cell Regulation · doi:10.1091/mbc.2.12.965 · Cited by 487
Self-citation
Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus E1A-associated p33 kinase
Tsai, L., Harlow, E., & Meyerson, M. M. (1991) · Nature · doi:10.1038/353174a0 · Cited by 459
Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases.
Gonzalez, F. A., Raden, D. L., & Davis, R. J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54548-8 · Cited by 448
Definition of a consensus sequence for peptide substrate recognition by p44mpk, the meiosis-activated myelin basic protein kinase
Clark‐Lewis, I., Sanghera, J. S., & Pelech, S. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98601-1 · Cited by 400
Identification of multiple extracellular signal-regulated kinases (ERKs) with antipeptide antibodies.
Boulton, T. G., & Cobb, M. H. (1991) · Cell Regulation · doi:10.1091/mbc.2.5.357 · Cited by 390
Self-citation
Phosphotransferase and substrate binding mechanism of the cAMP‐dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5‐24).
Bossemeyer, D., Engh, R. A., Kinzel, V., Ponstingl, H., & Huber, R. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05725.x · Cited by 389
Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation.
Seger, R., Ahn, N. G., Boulton, T. G., Yancopoulos, G. D., Panayotatos, N., Radziejewska, E., Ericsson, L. H., Bratlien, R. L., Cobb, M. H., & Krebs, E. G. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.14.6142 · Cited by 336
Self-citation
Glucose-induced conformational change in yeast hexokinase.
Bennett, W. S., & Steitz, T. A. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.10.4848 · Cited by 308
The human CL100 gene encodes a Tyr/Thr-protein phosphatase which potently and specifically inactivates MAP kinase and suppresses its activation by oncogenic ras in Xenopus oocyte extracts.
Alessi, D. R., Smythe, C., & Keyse, S. M. (1993) · PubMed · Cited by 304
Isolation of cDNA clones coding for the catalytic subunit of mouse cAMP-dependent protein kinase.
Uhler, M. D., Carmichael, D. F., Lee, D. C., Chrivia, J. C., Krebs, E. G., & McKnight, G. S. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.5.1300 · Cited by 271
ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ.
Haycock, J. W., Ahn, N. G., Cobb, M. H., & Krebs, E. G. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.6.2365 · Cited by 261
Self-citation
[28] Software for a diffractometer with multiwire area detector
Howard, A. J., Nielsen, C., & Xuong, N. H. (1985) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(85)14030-9 · Cited by 259
Isolation and characterization of two growth factor-stimulated protein kinases that phosphorylate the epidermal growth factor receptor at threonine 669
Northwood, I. C., Gonzalez, F. A., Wartmann, M., Raden, D. L., & Davis, R. J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98612-6 · Cited by 209
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.
Hurley, J. H., Thorsness, P. E., Ramalingam, V., Helmers, N. S., Koshland, D. E., & Stroud, R. M. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.22.8635 · Cited by 207
A template for the protein kinase family
Taylor, S. S., Knighton, D. R., Zheng, J., Sowadski, J. M., Gibbs, C. S., & Zoller, M. J. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)80001-r · Cited by 194
Dephosphorylation and inactivation of the mitogen-activated protein kinase by a mitogen-induced Thr/Tyr protein phosphatase
Zheng, C., & Guan, K. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85396-6 · Cited by 170
A dominant-negative mutant of raf blocks mitogen-activated protein kinase activation by growth factors and oncogenic p21ras.
Schaap, D., van der Wal, J., Howe, L. R., Marshall, C., & BLITTERSWIJK, W. J. V. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80719-4 · Cited by 160
Epidermal growth factor (EGF) receptor T669 peptide kinase from 3T3-L1 cells is an EGF-stimulated "MAP" kinase.
Takishima, K., Griswold‐Prenner, I., Ingebritsen, T. S., & Rosner, M. R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.6.2520 · Cited by 159
Mapping protein dynamics by X-ray diffraction
Ringe, D., & Petsko, G. A. (1985) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(85)90002-1 · Cited by 155
Eukaryotic protein kinases
Hanks, S. K. (1991) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(91)90035-r · Cited by 137
Nerve growth factor and fibroblast growth factor selectively activate a protein kinase that phosphorylates high molecular weight microtubule-associated proteins. Detection, partial purification, and characterization in PC12 cells.
Tsao, H., Aletta, J. M., & Greene, L. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55420-x · Cited by 116
Structural Basis for the Activation of Glycogen Phosphorylase b by Adenosine Monophosphate
Sprang, S. R., Withers, S. G., Goldsmith, E. J., Fletterick, R. J., & Madsen, N. B. (1991) · Science · doi:10.1126/science.1962195 · Cited by 111
Self-citation
Evidence that extracellular signal-regulated kinases are the insulin-activated Raf-1 kinase kinases.
Lee, R., Cobb, M. H., & Blackshear, P. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48399-8 · Cited by 104
Self-citation
Map Kinases Erk1 And Erk2: Pleiotropic Enzymes In A Ubiquitous Signaling Network
Robbins, D. J., Zhen, E., Cheng, M. M., Xu, S., Ebert, D. J., & Cobb, M. H. (1994) · Advances in cancer research · doi:10.1016/s0065-230x(08)60399-1 · Cited by 72
Self-citation
Structure of the mammalian catalytic subunit of cAMP-dependent protein kinase and an inhibitor peptide displays an open conformation
Karlsson, R., Zheng, J., Xuong, N., Taylor, S. S., & Sowadski, J. M. (1993) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444993002306 · Cited by 65
Identification of Tyr-185 as the site of tyrosine autophosphorylation of recombinant mitogen-activated protein kinase p42mapk.
Rossomando, A. J., Wu, J., Michel, H., Shabanowitz, J., Hunt, D. F., Weber, M. J., & Sturgill, T. W. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.13.5779 · Cited by 61
Domain motions in proteins
Schulz, G. E. (1991) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(91)90082-5 · Cited by 57
Crystallization and Preliminary X-ray Studies of Extracellular Signal-regulated Kinase-2/MAP Kinase with an Incorporated His-tag
Zhang, F. P. Y., Robbins, D. J., Cobb, M. H., & Goldsmith, E. J. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1532 · Cited by 31
Self-citation

Research works printed but not linked: 4

Alessi, D. R., Smythe, C. & Keyse, S. M. Oncogene 8, 2015–2020 (1993).
Karlsson, R., Zheng, J., Xuong, N.-H., Taylor, S. S. & Sowadski, J. M. Acta crystallogr. D49, 381–388 (1993).
Steigemann, W. PROTEIN, A Program System for the Crystal Structure Analysis of Proteins (Max-Planck-Institute für Biochimie, Martinsried, Germany, 1989).
Wang, B.-C. in Meth. Enzym. (eds Hirs, C. H. & Wyckoff, H. W.) Vol. 115, 90–112 (Academic, New York, 1985).

Sorted by citations

Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*
Pearson, G. W., Robinson, F. L., Gibson, T. B., Xu, B.-E., Karandikar, M. S., Berman, K. S., & Cobb, M. H. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.2.0428 · Cited by 4,111
Self-citation
Mutation of the mouse klotho gene leads to a syndrome resembling ageing
Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837
A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
Lee, J. C., Laydon, J. T., McDonnell, P., Gallagher, T. F., Kumar, S., Green, D., McNulty, D. E., Blumenthal, M. J., Keys, J., vatter, S. W. L., et al. (1994) · Nature · doi:10.1038/372739a0 · Cited by 3,266
A MAP Kinase Targeted by Endotoxin and Hyperosmolarity in Mammalian Cells
Han, J., Lee, J. D., Bibbs, L., & Ulevitch, R. J. (1994) · Science · doi:10.1126/science.7914033 · Cited by 2,647
The Conformational Plasticity of Protein Kinases
Huse, M., & Kuriyan, J. (2002) · Cell · doi:10.1016/s0092-8674(02)00741-9 · Cited by 1,760

See all 602

Authors: Zhang, F., Strand, A., Robbins, D., Cobb, M. H., & Goldsmith, E. J.
Affiliations: The University of Texas Southwestern Medical Center (US)
Howard Hughes Medical Institute (US)
ORCID: Robbins, David
Cobb, Melanie H.
Goldsmith, Elizabeth J.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1994-02
Volume: 367
Issue: 6465
Pages: 704-711
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/367704a0
OpenAlex: W1994954884
Cited by: 592
References: 52
Citations by year: 2026: 7 · 2025: 5 · 2024: 6 · 2023: 14 · 2022: 4 · 2021: 6 · 2020: 11 · 2019: 16 · 2018: 4 · 2017: 3 · 2016: 9 · 2015: 14 · 2014: 14 · 2013: 10 · 2012: 14
FWCI: 20.95
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords: ERK2, mitogen-activated protein kinase, protein kinase structure, peptide binding site, conformational change, Ras/Raf signaling, kinase activation
MeSH terms: Adenosine Triphosphate, Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Phosphorylation, Protein Conformation, Substrate Specificity, Sequence Alignment, Calcium-Calmodulin-Dependent Protein Kinases, Crystallography, X-Ray, Mitogen-Activated Protein Kinase 1

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

Atomic structure of the MAP kinase ERK2 at 2.3 A resolution

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