PMID- 19273288
OWN - NLM
STAT- MEDLINE
DCOM- 20090407
LR  - 20220227
IS  - 2768-6698 (Electronic)
IS  - 2768-6698 (Linking)
VI  - 14
IP  - 9
DP  - 2009 Jan 1
TI  - MLL histone methylases in gene expression, hormone signaling and cell cycle.
PG  - 3483-95
LID - 10.2741/3466 [doi]
AB  - Histone methyl-transferases (HMTs) are key enzymes that post-translationally 
      methylate nuclear histone proteins and play critical roles in gene expression, 
      epigenetic regulation and diseases in eukaryotic organisms. Mixed lineage 
      leukemias (MLLs) are human HMTs that specifically methylate histone H3 at 
      lyisine-4 and regulate gene activation. MLLs are also well known to be rearranged 
      often in acute myeloid and lymphoid leukemias. Human encodes several MLLs that 
      have similar enzymatic activities but diverse functions. Herein, we have reviewed 
      the recent advances in understanding the diverse functions of MLL family of HMTs 
      in gene regulation, hormone signaling and cell cycle regulation in human.
FAU - Ansari, Khairul I
AU  - Ansari KI
AD  - Gene Regulation and Disease Laboratory, Department of Chemistry and Biochemistry, 
      The University of Texas at Arlington, Arlington, Texas 76019, USA.
FAU - Mishra, Bibhu P
AU  - Mishra BP
FAU - Mandal, Subhrangsu S
AU  - Mandal SS
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20090101
PL  - Singapore
TA  - Front Biosci (Landmark Ed)
JT  - Frontiers in bioscience (Landmark edition)
JID - 101612996
RN  - 0 (Hormones)
RN  - EC 2.1.1.- (Histone Methyltransferases)
RN  - EC 2.1.1.- (Protein Methyltransferases)
RN  - EC 2.1.1.43 (Histone-Lysine N-Methyltransferase)
SB  - IM
MH  - *Cell Cycle
MH  - *Gene Expression
MH  - Histone Methyltransferases
MH  - Histone-Lysine N-Methyltransferase
MH  - Hormones/*metabolism/*physiology
MH  - Methylation
MH  - Protein Methyltransferases/*metabolism
MH  - *Signal Transduction
RF  - 95
EDAT- 2009/03/11 09:00
MHDA- 2009/04/08 09:00
CRDT- 2009/03/11 09:00
PHST- 2009/03/11 09:00 [entrez]
PHST- 2009/03/11 09:00 [pubmed]
PHST- 2009/04/08 09:00 [medline]
AID - 3466 [pii]
AID - 10.2741/3466 [doi]
PST - epublish
SO  - Front Biosci (Landmark Ed). 2009 Jan 1;14(9):3483-95. doi: 10.2741/3466.