|1.||Sukegawa, Yasushi: 3 articles (10/2014 - 11/2012)|
|2.||Okuno, Kiyotaka: 3 articles (10/2014 - 11/2012)|
|3.||Inoue, Keisuke: 3 articles (10/2014 - 11/2012)|
|4.||Sugiura, Fumiaki: 3 articles (10/2014 - 11/2012)|
|5.||Kogita, Akihiro: 2 articles (10/2014 - 11/2013)|
|6.||Yoshioka, Yasumasa: 2 articles (10/2014 - 11/2013)|
|7.||Hida, Jinichi: 2 articles (10/2014 - 11/2013)|
|8.||Kurahashi, Hiroki: 2 articles (01/2013 - 08/2004)|
|9.||Ohye, Tamae: 2 articles (01/2013 - 08/2004)|
|10.||Valente, Valeria: 2 articles (01/2013 - 01/2009)|
|1.||Colorectal Neoplasms (Colorectal Cancer)
11/01/2012 - "A new study has been planned in order to obtain more immunological responses, and we have started a clinical trial of vaccines against multiple peptides[RNF43, TOMM34, forkhead box protein M1(FOXM1), maternal embryonic leucine zipper kinase(MELK), holliday junction recognition protein(HJURP), vascular endothelial growth factor receptor (VEGFR)1, and VEGFR2]by using UFT/LV for the treatment of advanced or recurrent colorectal cancer."
11/01/2013 - "We started a clinical trial of vaccines against multiple peptides (RNF43, TOMM34, forkhead box protein M1 [FOXM1], maternal embryonic leucine zipper kinase [MELK], holliday junction recognition protein[HJURP], vascular endothelial growth factor receptor 1[VEGFR1], and VEGFR2) for the treatment of advanced or recurrent colorectal cancer. "
01/15/2012 - "SMARCAL1 catalyzes fork regression and Holliday junction migration to maintain genome stability during DNA replication."
09/08/2010 - "It functions to separate double Holliday junction DNA without genetic exchange as a component of the "dissolvasome," which also includes topoisomerase IIIα and the RMI (RecQ-mediated genome instability) subcomplex (RMI1 and RMI2). "
09/01/2014 - "Holliday junction processing enzymes as guardians of genome stability."
12/01/2008 - "In human cells and in Saccharomyces cerevisiae, BLAP75/Rmi1 acts together with BLM/Sgs1 and TopoIIIalpha/Top3 to maintain genome stability by limiting crossover (CO) formation in favour of NCO events, probably through the dissolution of double Holliday junction intermediates (dHJ). "
02/01/2015 - "This review explores the properties of these pairing and annealing proteins, and highlights their roles in complex recombination processes including the double Holliday junction (DhJ) formation, synthesis-dependent strand annealing, and single-strand annealing pathways--DNA transactions that are critical both for genome stability in individual organisms and for the evolution of species."
|4.||Werner Syndrome (Werner's Syndrome)
07/01/2010 - "Telomeric protein TRF2 protects Holliday junctions with telomeric arms from displacement by the Werner syndrome helicase."
09/05/2008 - "The Werner syndrome protein binds replication fork and holliday junction DNAs as an oligomer."
03/01/2007 - "Correction of proliferation and drug sensitivity defects in the progeroid Werner's Syndrome by Holliday junction resolution."
01/01/2007 - "Replication fork regression in vitro by the Werner syndrome protein (WRN): holliday junction formation, the effect of leading arm structure and a potential role for WRN exonuclease activity."
07/01/2000 - "Werner's syndrome protein (WRN) migrates Holliday junctions and co-localizes with RPA upon replication arrest."
11/15/1991 - "The data are consistent with a model in which vaccinia topoisomerase catalyzes reciprocal strand transfer, leading to the formation of a nonmigrating Holliday junction, the resolution of which can lead to excisive recombination."
07/15/2000 - "Resolution of a Holliday junction by vaccinia topoisomerase requires a spacer DNA segment 3' of the CCCTT/ cleavage sites."
11/30/2007 - "Vaccinia encodes an enzyme, A22 resolvase, which is known to be active on four-stranded DNA junctions (Holliday junctions) or Holliday junction-like structures containing three of the four strands. "
|3.||Vascular Endothelial Growth Factor Receptors (VEGF Receptors)
|5.||DNA (Deoxyribonucleic Acid)
|6.||Cruciform DNA (Holliday Junctions)
|7.||Proteins (Proteins, Gene)
|9.||Staphylococcal Protein A (A, Protein)