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enEnglish daDanish
1 word
modulate modulere
enEnglish deGerman
1 word
modulate modulieren
2 words
to modulate abstimmen
to modulate anpassen
to modulate modulieren
enEnglish esSpanish
1 word
modulate modular
enEnglish frFrench
1 word
modulate moduler
enEnglish ioIdo
1 word
modulate modulacar
enEnglish ptPortuguese
1 word
modulate modular
enEnglish ruRussian
1 word
modulate модулировать
Interferon Signaling Modulation Pathway definition: Signaling by interferon-gamma stimulates anti-viral responses and tumor suppression through the heterodimeric interferon-gamma receptor. Signaling is initiated by binding of interferon-gamma to its receptor, activating the receptor-associated JAK2 tyrosine kinase to phosphorylate STAT transcription factors that activate interferon responsive genes. Molecular chaperones that modulate or alter protein folding interact with different components of the interferon signaling pathway. One chaperone that modulates interferon signaling is hTid-1, a member of the DnaJ family of chaperones and a co-chaperone for the heat shock protein Hsp70, another molecular chaperone. hTid-1 was found in a two-hybrid screen to bind to JAK2 and also to interact with the interferon-gamma receptor. In addition, hTid-1 and JAK2 also interact with Hsp70. Overexpression of hTid-1 represses transcriptional activation by interferon-gamma and Hsp70 dissociates from these proteins when interferon is added to cells, suggesting that Hsp70 holds Jak2 in an inactive conformation prior to ligand activation, and is released in the presence of agonist to allow the activation of Jak-2 and downstream pathways. hTid-1 and Hsp-70 interact with other signaling proteins as well. One of these is Tax, a protein encoded by the HTLV-1 virus that binds to hTid-1. hTid-1 also represses NF-kB activation by blocking the phosphorylation and inactivation of I-kappaB by the IkappaB kinase beta. Hsp70 plays a significant role in protein unfolding for entry into mitochondria and also interacts with tumor suppressor gene products to produce their anti-proliferative activity. One of the actions of interferon is to induce apoptosis of infected target cells, in part through a mitochondrial dependent mechanism. An interaction between interferon signaling and Hsp70 may alter this mitochondrial apoptosis pathway, perhaps playing a role in interferon-mediated apoptosis of infected or transformed cells. The HTLV-1 Tax protein that interacts with Hsp70 blocks mitochondrial induced apoptosis, providing a protection against interferon-mediated cellular defenses. (BioCarta)
Sumoylation in Modulation of CtBP-Dependent Gene Response Pathway definition: Covalent attachment of one eukaryotic protein to another is a prominent posttranslational modification and Ubiquitin is the most familiar of the protein modifiers. Recently a new group of ubiquitin-like (Ubl) proteins have come to light. One of the most intriguing of them is SUMO (small ubiquitin-like modifier, ~12kDa) also known as Sentrin. SUMO family has been described in vertebrates: SUMO-1 and the closest homologs SUMO-2 and SUMO-3. SUMO have been shown to bind and regulate mammalian SP-RINGs (such as Mdm2, PIAS and PML), RanGAP1, RanBP2, p53, p73, HIPK2, TEL, c-Jun, CtBP, Fas, Daxx, TNFRI, Topo-I, Topo-II, WRN, Sp100, IkB-alpha, Androgen receptor (AR), GLUT1/4, Drosophila Ttk69, Dorsal, CaMK, yeast Septins, and viral CMV-IE1/2, EBV-BZLF1, HPV/BPV-E1. In the case of the transcription co-repressor CtBP, which can be recruited to the target promoter via interaction with a conserved PxDLS motif in the interacting repressor, CtBP SUMOylation profoundly affected its subcellular localization. SUMOylation occurred at a single Lys residue, Lys428, of CtBP1. Mutating Lys428 into Arg (K428R) shifted CtBP1 from the nucleus to the cytoplasm, while it had little effect on its interaction with the PxDLS motif. The K428R mutation also abolished the ability of CtBP1 to repress the E-cadherin promoter activity. Consistent with the known inhibitory effect of nNOS on the nuclear accumulation of CtBP1, PDZ domain of nNOS inhibits the SUMOylation of CtBP1. The current data indicates that SUMOylation can regulate CtBP1-dependent transcriptional repression. (BioCarta)
modulieren definition: abwandeln abändern verändern

Published in vitro evidence has suggested that other members of the calmodulin super-family, in particular the neuronal calcium sensor (NCS) proteins, can similarly modulate calcineurin activity.

Daniel J. Fitzgerald et al.

Biochimica et Biophysica Acta 1780 (2), 01 Feb 2008

Results from these experiments indicate that NCS-1 was not able to detectably modulate calcineurin/NFAT signalling in a live mammalian cell system, findings that are consistent with the idea that calmodulin and not NCS-1 or other NCS family proteins is the physiologically relevant modulator of calcineurin activity.

Daniel J. Fitzgerald et al.

Biochimica et Biophysica Acta 1780 (2), 01 Feb 2008

Secondly, NCS proteins could feasibly interact with CaM targets in biochemically distinct ways to modulate their activities in specific, CaM independent, manners leading to the overall generation of unique physiological endpoints.

Daniel J. Fitzgerald et al.

Biochimica et Biophysica Acta 1780 (2), 01 Feb 2008

The possibility remains that there may be some level of interplay between NCS proteins and CaM within protein complexes, exemplified by observations that both CaM and CaBP1 interact with IP3-receptors [40,48,49] , that both NCS-1 and CaM are able to interact with Ca 2+ channels [50] and G-protein coupled receptor kinases [34,51,52] and that CaM, NCS-1 and CaBP1 have all been shown to modulate the activity of the transient receptor potential channel, TRPC5 [35] .

Daniel J. Fitzgerald et al.

Biochimica et Biophysica Acta 1780 (2), 01 Feb 2008

In addition, the data showed that the interactions with MCM modulate the autophosphorylation of Cdc6-1 and -2.

Rajesh Kasiviswanathan et al.

Nucleic Acids Research 33 (15), 2005

964 further examples >>

Neuronal calcium sensor proteins are unable to modulate NFAT activation in mammalian cells

Daniel J. Fitzgerald et al.

Biochimica et Biophysica Acta , 01 Feb 2008

Interactions between the archaeal Cdc6 and MCM proteins modulate their biochemical properties

Rajesh Kasiviswanathan et al.

Nucleic Acids Research , 2005

Synovial microparticles from arthritic patients modulate chemokine and cytokine release by synoviocytes

René J Berckmans et al.

Arthritis Research & Therapy , 2005

HLA-C locus alleles may modulate the clinical expression of psoriatic arthritis

Ruben Queiro et al.

Arthritis Research & Therapy , 2006

Individual preferences modulate incentive values: Evidence from functional MRI

Susan Koeneke et al.

Behavioral and Brain Functions : BBF , 25 Nov 2008

NSAIDs Modulate CDKN2A, TP53, and DNA Content Risk for Progression to Esophageal Adenocarcinoma

Patricia C Galipeau et al.

PLoS Medicine , 01 Feb 2007

Nutrient-Regulated Antisense and Intragenic RNAs Modulate a Signal Transduction Pathway in Yeast

Masafumi Nishizawa et al.

PLoS Biology , 01 Dec 2008

Chimeric peptide nucleic acid compounds modulate splicing of the bcl-x gene in vitro and in vivo

Jeremy E. Wilusz et al.

Nucleic Acids Research , 2005

IL-1β and IL-6 modulate apolipoprotein E gene expression in rat hepatocyte primary culture

Agnes Ribeiro et al.

Mediators of Inflammation , 1992

Anaesthetics modulate tumour necrosis factor α: effects of L-carnitine supplementation in surgical patients. Preliminary results.

Giovanna Delogu et al.

Mediators of Inflammation , 1993

959 further publications >>