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Cited by 402

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Inhibition of the Mitogen-Activated Protein Kinase Kinase Superfamily by a Yersinia Effector

Orth, Kim, Palmer, Lance E., Bao, Zhao Qin, Stewart, Scott, Rudolph, Amy E., Bliska, James B., Dixon, Jack E.·1999·Science

Abstract

The bacterial pathogen Yersinia uses a type III secretion system to inject several virulence factors into target cells. One of the Yersinia virulence factors, YopJ, was shown to bind directly to the superfamily of MAPK (mitogen-activated protein kinase) kinases (MKKs) blocking both phosphorylation and subsequent activation of the MKKs. These results explain the diverse activities of YopJ in inhibiting the extracellular signal–regulated kinase, c-Jun amino-terminal kinase, p38, and nuclear factor kappa B signaling pathways, preventing cytokine synthesis and promoting apoptosis. YopJ-related proteins that are found in a number of bacterial pathogens of animals and plants may function to block MKKs so that host signaling responses can be modulated upon infection.

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Metadata

Authors
Orth, K., Palmer, L. E., Bao, Z. Q., Stewart, S., Rudolph, A. E., Bliska, J. B., & Dixon, J. E.
Venue
Science
Published
1999-09-17
Volume
285
Issue
5435
Pages
1920-1923
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1974405307
Cited by
402
References
2
FWCI
15.37
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Inhibition of the Mitogen-Activated Protein Kinase Kinase Superfamily by a Yersinia Effector. https://app.cochat.ai/papers/10.1126/science.285.5435.1920
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Orth, K., Palmer, L. E., Bao, Z. Q., Stewart, S., Rudolph, A. E., Bliska, J. B., & Dixon, J. E. (1999). Inhibition of the Mitogen-Activated Protein Kinase Kinase Superfamily by a Yersinia Effector. Science. https://doi.org/10.1126/science.285.5435.1920

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