LEADER 01000caa a22002652 4500
001 NLM222685905
003 DE-627
005 20250214154433.0
007 cr uuu---uuuuu
008 231224s2013 xx |||||o 00| ||eng c
024 7 |a 10.1016/j.clim.2012.09.009  |2 doi 
028 5 2 |a pubmed25n0742.xml 
035 |a (DE-627)NLM222685905 
035 |a (NLM)23158694 
035 |a (PII)S1521-6616(12)00234-3 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Markopoulou, Anastasia  |e verfasserin  |4 aut 
245 1 0 |a Small molecules in the treatment of systemic lupus erythematosus 
264 1 |c 2013 
336 |a Text  |b txt  |2 rdacontent 
337 |a ƒaComputermedien  |b c  |2 rdamedia 
338 |a ƒa Online-Ressource  |b cr  |2 rdacarrier 
500 |a Date Completed 23.10.2013 
500 |a Date Revised 18.03.2024 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a Copyright © 2012 Elsevier Inc. All rights reserved. 
520 |a Advances in the understanding of the cellular biological events that underlie systemic lupus erythematosus (SLE) have led to the identification of key molecules and signaling pathways that are aberrantly expressed. The parallel development of small molecule drugs that inhibit or interfere with the specific perturbations identified, offers perspective for more rational, effective and less toxic therapy. In this review, we present data from preclinical and clinical studies of such emerging novel therapies with a particular focus on kinase inhibitors and other compounds that modulate signal transduction. Moreover, we highlight the use of chromatin-modifying medications, bringing attention to the central role of epigenetics in SLE pathogenesis 
650 4 |a Journal Article 
650 4 |a Research Support, N.I.H., Extramural 
650 4 |a Review 
650 4 |a HDAC inhibitors 
650 4 |a Jak 
650 4 |a Kinase inhibitors 
650 4 |a Syk 
650 4 |a Systemic lupus erythematosus 
650 7 |a Intracellular Signaling Peptides and Proteins  |2 NLM 
650 7 |a Phosphoinositide-3 Kinase Inhibitors  |2 NLM 
650 7 |a Proteasome Inhibitors  |2 NLM 
650 7 |a Protein Kinase Inhibitors  |2 NLM 
650 7 |a Protein-Tyrosine Kinases  |2 NLM 
650 7 |a EC 2.7.10.1  |2 NLM 
650 7 |a Agammaglobulinaemia Tyrosine Kinase  |2 NLM 
650 7 |a EC 2.7.10.2  |2 NLM 
650 7 |a Janus Kinases  |2 NLM 
650 7 |a EC 2.7.10.2  |2 NLM 
650 7 |a SYK protein, human  |2 NLM 
650 7 |a EC 2.7.10.2  |2 NLM 
650 7 |a Syk Kinase  |2 NLM 
650 7 |a EC 2.7.10.2  |2 NLM 
650 7 |a rho-Associated Kinases  |2 NLM 
650 7 |a EC 2.7.11.1  |2 NLM 
650 7 |a Calcium-Calmodulin-Dependent Protein Kinase Type 4  |2 NLM 
650 7 |a EC 2.7.11.17  |2 NLM 
700 1 |a Kyttaris, Vasileios C  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Clinical immunology (Orlando, Fla.)  |d 1999  |g 148(2013), 3 vom: 16. Sept., Seite 359-68  |w (DE-627)NLM098196855  |x 1521-7035  |7 nnns 
773 1 8 |g volume:148  |g year:2013  |g number:3  |g day:16  |g month:09  |g pages:359-68 
856 4 0 |u http://dx.doi.org/10.1016/j.clim.2012.09.009  |3 Volltext 
912 |a GBV_USEFLAG_A 
912 |a SYSFLAG_A 
912 |a GBV_NLM 
912 |a GBV_ILN_11 
912 |a GBV_ILN_24 
912 |a GBV_ILN_350 
951 |a AR 
952 |d 148  |j 2013  |e 3  |b 16  |c 09  |h 359-68