Claudia Wietek
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Claudia Wietek has a total of 6 co-authors. Here are the top co-authors by number of shared publications:
- Aisling Dunne
School of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, University of Dublin, Dublin, Ireland
1 shared publication Caroline Jefferies
1 shared publicationLuke A.J. O’neill
School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, Ireland
1 shared publication- Luke Anthony John O'NEill
Trinity College Dublin
1 shared publication Michael Edjeback
1 shared publicationPearl Gray
1 shared publication
Latest Publications
- 1 July 2007
- Published by Elsevier in Trends in Biochemical Sciences
- Vol. 32 (7) , 311-319
Diversity and regulation in the NF-κB system
- 1 July 2007
- Published by Elsevier in Trends in Biochemical Sciences
- Vol. 32 (7) , 311-319
Diversity and regulation in the NF-κB system
- 1 February 2003
- Published by SAGE Publications in Innate Immunity
- Vol. 9 (1) , 55-59
Mal and MyD88: adapter proteins involved in signal transduction by Toll-like receptors
Signal transduction processes activated by Toll-like receptors (TLRs) include the important transcription factor NF-kappaB and 2 MAP kinases, p38 and Jun N-terminal kinase. These signals ultimately give rise to increased expression of a multitude of pro-inflammatory proteins. Receptor-proximal proteins involved in signalling by all TLRs include the adapter MyD88, 3 IRAKs (IRAK-4, IRAK and IRAK-2), Tollip, Traf-6 and TAK-1. Differences between signals generated by TLRs are emerging, with both TLR4 and TLR2 signalling requiring an additional adapter termed MyD88-adapter-like (Mal; also known as TIRAP). MyD88 and Mal both have a homologous Toll/IL-1 receptor (TIR) domain although they differ in their N-termini, with MyD88 possessing a death domain. In addition, structural models reveal marked differences in surface charges which, when taken with surface charge differences between TLR2 and TLR4 TIR domains, may indicate that TLR4 but not TLR2 recruits Mal directly. Another difference is that Mal can become phosphorylated. Future studies on Mal will reveal specificities in signal transduction by different TLRs, which may ultimately provide molecular explanations for specificities in the innate immune response to infection.
- 1 February 2003
- Published by SAGE Publications in Innate Immunity
- Vol. 9 (1) , 55-59
Mal and MyD88: adapter proteins involved in signal transduction by Toll-like receptors
Signal transduction processes activated by Toll-like receptors (TLRs) include the important transcription factor NF-kappaB and 2 MAP kinases, p38 and Jun N-terminal kinase. These signals ultimately give rise to increased expression of a multitude of pro-inflammatory proteins. Receptor-proximal proteins involved in signalling by all TLRs include the adapter MyD88, 3 IRAKs (IRAK-4, IRAK and IRAK-2), Tollip, Traf-6 and TAK-1. Differences between signals generated by TLRs are emerging, with both TLR4 and TLR2 signalling requiring an additional adapter termed MyD88-adapter-like (Mal; also known as TIRAP). MyD88 and Mal both have a homologous Toll/IL-1 receptor (TIR) domain although they differ in their N-termini, with MyD88 possessing a death domain. In addition, structural models reveal marked differences in surface charges which, when taken with surface charge differences between TLR2 and TLR4 TIR domains, may indicate that TLR4 but not TLR2 recruits Mal directly. Another difference is that Mal can become phosphorylated. Future studies on Mal will reveal specificities in signal transduction by different TLRs, which may ultimately provide molecular explanations for specificities in the innate immune response to infection.