Photoregulated tyrosinase gene in Polyporus arcularius

Mycoscience ◽  
2007 ◽  
Vol 48 (1) ◽  
pp. 34-41 ◽  
Author(s):  
Satoshi Kanda ◽  
Seita Masumoto ◽  
Kaori Nakano ◽  
Tsutomu Morinaga ◽  
Tadanori Aimi ◽  
...  
Keyword(s):  
Tyrosinase Gene ◽  
Polyporus Arcularius

Cloning, sequence and expression of the tyrosinase gene from Streptomyces lavendulae MA406 A-1

1993 ◽  
Vol 76 (5) ◽  
pp. 345-355 ◽  
Author(s):  
Shinichi Kawamoto ◽  
Mitinobu Nakamura ◽  
Shigetaka Yashima
Keyword(s):  
Tyrosinase Gene ◽  
Streptomyces Lavendulae

The R402Q mutation of the Tyrosinase Gene: Lack of Association with oculocutaneous albinism type 1 (OCA1).

2004 ◽  
Vol 17 (4) ◽  
pp. 427-427
Author(s):  
R. A. King ◽  
J. Pietsch ◽  
M. J. Brott ◽  
S. Savage ◽  
J. P. Fryer ◽  
...  
Keyword(s):  
Oculocutaneous Albinism ◽  
Tyrosinase Gene

scholarly journals Ascidian tyrosinase gene: Its unique structure and expression in the developing brain

1997 ◽  
Vol 208 (3) ◽  
pp. 363-374 ◽  
Author(s):  
Shigeru Sato ◽  
Hiroshi Masuya ◽  
Takaharu Numakunai ◽  
Noriyuki Satoh ◽  
Kazuho Ikeo ◽  
...  
Keyword(s):  
Developing Brain ◽  
Unique Structure ◽  
Tyrosinase Gene

scholarly journals A frequent tyrosinase gene mutation in classic, tyrosinase-negative (type IA) oculocutaneous albinism.

1990 ◽  
Vol 87 (9) ◽  
pp. 3255-3258 ◽  
Author(s):  
L. B. Giebel ◽  
K. M. Strunk ◽  
R. A. King ◽  
J. M. Hanifin ◽  
R. A. Spritz
Keyword(s):  
Gene Mutation ◽  
Oculocutaneous Albinism ◽  
Negative Type ◽  
Tyrosinase Gene ◽  
Type Ia

Rescue of the albino phenotype by introduction of a functional tyrosinase gene into mice.

1990 ◽  
Vol 9 (9) ◽  
pp. 2819-2826 ◽  
Author(s):  
F. Beermann ◽  
S. Ruppert ◽  
E. Hummler ◽  
F. X. Bosch ◽  
G. Müller ◽  
...  
Keyword(s):  
Tyrosinase Gene ◽  
Albino Phenotype

scholarly journals An HLA-A2-restricted tyrosinase antigen on melanoma cells results from posttranslational modification and suggests a novel pathway for processing of membrane proteins.

1996 ◽  
Vol 183 (2) ◽  
pp. 527-534 ◽  
Author(s):  
J C Skipper ◽  
R C Hendrickson ◽  
P H Gulden ◽  
V Brichard ◽  
A Van Pel ◽  
...  
Keyword(s):  
Posttranslational Modification ◽  
Melanoma Cells ◽  
Amino Acid Sequences ◽  
Class I ◽  
Antigenic Peptides ◽  
Peptide Antigens ◽  
Mhc Molecules ◽  
Tyrosinase Gene ◽  
Histocompatibility Complex ◽  
Natural Peptide

T lymphocytes recognize antigens consisting of peptides presented by class I and II major histocompatibility complex (MHC) molecules. The peptides identified so far have been predictable from the amino acid sequences of proteins. We have identified the natural peptide target of a CTL clone that recognizes the tyrosinase gene product on melanoma cells. The peptide results from posttranslational conversion of asparagine to aspartic acid. This change is of central importance for peptide recognition by melanoma-specific T cells, but has no impact on peptide binding to the MHC molecule. This posttranslational modification has not been previously described for any MHC-associated peptide and represents the first demonstration of posttranslational modification of a naturally processed class I-associated peptide. This observation is relevant to the identification and prediction of potential peptide antigens. The most likely mechanism for production of this peptide leads to the suggestion that antigenic peptides can be derived from proteins that are translated into the endoplasmic reticulum.

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