Lucidenic acid O and lactone, new terpene inhibitors of eukaryotic DNA polymerases from a basidiomycete, ganoderma lucidum

1999 ◽  
Vol 7 (9) ◽  
pp. 2047-2052 ◽  
Author(s):  
Yoshiyuki Mizushina ◽  
Naoko Takahashi ◽  
Linda Hanashima ◽  
Hiroyuki Koshino ◽  
Yasuaki Esumi ◽  
...  
2020 ◽  
Vol 66 (4) ◽  
pp. 635-655 ◽  
Author(s):  
Narottam Acharya ◽  
Prashant Khandagale ◽  
Shweta Thakur ◽  
Jugal Kishor Sahu ◽  
Bhabasha Gyanadeep Utkalaja

2002 ◽  
Vol 63 (3) ◽  
pp. 399-407 ◽  
Author(s):  
Yoshiyuki Mizushina ◽  
Chikako Murakami ◽  
Keisuke Ohta ◽  
Hirosato Takikawa ◽  
Kenji Mori ◽  
...  

2003 ◽  
Vol 66 (4) ◽  
pp. 541-550 ◽  
Author(s):  
Chikako Murakami ◽  
Masaharu Takemura ◽  
Hiromi Yoshida ◽  
Fumio Sugawara ◽  
Kengo Sakaguchi ◽  
...  

Author(s):  
Brigette Tippin ◽  
Myron F. Goodman

The mechanism of somatic hypermutation of the immunoglobulin genes remains a mystery after nearly 30 years of intensive research in the field. While many clues to the process have been discovered in terms of the genetic elements required in the immunoglobulin genes, the key enzymatic players that mediate the introduction of mutations into the variable region are unknown. The recent wave of newly discovered eukaryotic DNA polymerases have given a fresh supply of potential candidates and a renewed vigour in the search for the elusive mutator factor governing affinity maturation. In this paper, we discuss the relevant genetic and biochemical evidence known to date regarding both somatic hypermutation and the new DNA polymerases and address how the two fields can be brought together to identify the strongest candidates for further study. In particular we discuss evidence for the in vitro biochemical misincorporation properties of human Rad30B/Pol ι and how it compares to the in vivo somatic hypermutation spectra.


Cell ◽  
1989 ◽  
Vol 59 (1) ◽  
pp. 219-228 ◽  
Author(s):  
Antonio Bernad ◽  
Luis Blanco ◽  
JoséM. Lázaro ◽  
Gil Martín ◽  
Margarita Salas

2001 ◽  
Vol 66 (11) ◽  
pp. 1698-1706 ◽  
Author(s):  
Gabriel Birkuš ◽  
Ivan Votruba ◽  
Miroslav Otmar ◽  
Antonín Holý

The inhibitory and/or substrate activity of 1-[(S)-3-hydroxy-2-(phosphonomethoxy)propyl]cytosine [(S)-HPMPC, cidofovir, Vistide™] diphosphate towards eukaryotic DNA polymerases α, δ and ε* was examined. Cidofovir diphosphate is a weak competitive inhibitor of the above enzymes, approximately 3 to 7 times weaker than its adenine analogue (S)-HPMPApp. The enzymes also catalyze incorporation of (S)-HPMPC into DNA; after insertion of one (S)-HPMPC residue into DNA, another dNMP residue may incorporate. DNA polymerase δ and ε* can successively accommodate in the growing chain two (S)-HPMPC residues at the maximum, whereas pol α up to three residues.


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