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TYW1 gene
Known as:
TYW1A
, MGC23001
, tRNA-yW synthesizing protein 1 homolog A (S. cerevisiae)
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National Institutes of Health
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2017
Review
2017
On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes
E. Mulliez
,
V. Duarte
,
Simon Arragain
,
M. Fontecave
,
M. Atta
Front. Chem.
2017
Corpus ID: 16577340
The canonical CysXXXCysXXCys motif is the hallmark of the Radical-SAM superfamily. This motif is responsible for the ligation of…
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Review
2016
Review
2016
Radical S-Adenosylmethionine Enzymes in Human Health and Disease.
B. Landgraf
,
Erin L. McCarthy
,
S. Booker
Annual review of biochemistry
2016
Corpus ID: 27292290
Radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across…
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2014
2014
Xenogeneic Acellular Conjunctiva Matrix as a Scaffold of Tissue-Engineered Corneal Epithelium
Haifeng Zhao
,
Mingli Qu
,
Yao Wang
,
Zhenyu Wang
,
W. Shi
PloS one
2014
Corpus ID: 2552396
Amniotic membrane-based tissue-engineered corneal epithelium has been widely used in the reconstruction of the ocular surface…
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2012
2012
4-Demethylwyosine Synthase from Pyrococcus abyssi Is a Radical-S-adenosyl-l-methionine Enzyme with an Additional [4Fe-4S]+2 Cluster That Interacts with the Pyruvate Co-substrate*
Phanélie Perche-Létuvée
,
V. Kathirvelu
,
+10 authors
M. Atta
The Journal of Biological Chemistry
2012
Corpus ID: 9704703
Background: 4-Demethylwyosine synthase (TYW1) is a tRNA-modifying metalloenzyme involved in the biosynthesis of wyosine. Results…
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2011
2011
Pyruvate is the source of the two carbons that are required for formation of the imidazoline ring of 4-demethylwyosine.
A. Young
,
V. Bandarian
Biochemistry
2011
Corpus ID: 5421013
TYW1 catalyzes the condensation of N-methylguanosine with two carbon atoms from an unknown second substrate to form 4…
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2011
2011
Yap5 Protein-regulated Transcription of the TYW1 Gene Protects Yeast from High Iron Toxicity*
Liangtao Li
,
X. Jia
,
D. Ward
,
J. Kaplan
The Journal of Biological Chemistry
2011
Corpus ID: 30179717
Background: Yeast cells respond to high environmental iron by altering gene transcription. Results: The high iron-sensing…
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2007
2007
Structure of an archaeal TYW1, the enzyme catalyzing the second step of wye-base biosynthesis.
S. Goto-Ito
,
R. Ishii
,
+5 authors
S. Yokoyama
Acta crystallographica. Section D, Biological…
2007
Corpus ID: 23741684
Wye bases are tricyclic bases that are found in archaeal and eukaryotic tRNAs. The most modified wye base, wybutosine, which…
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Highly Cited
2007
Highly Cited
2007
Defining the extended substrate specificity of kallikrein 1-related peptidases
C. Borgoño
,
J. Gavigan
,
+4 authors
E. Diamandis
Biological chemistry
2007
Corpus ID: 8365909
Abstract Human kallikrein 1-related peptidases (KLKs) form a subfamily of 15 extracellular (chymo)tryptic-like serine proteases…
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Highly Cited
2007
Highly Cited
2007
Crystal structure of the radical SAM enzyme catalyzing tricyclic modified base formation in tRNA.
Yoko Suzuki
,
A. Noma
,
+4 authors
O. Nureki
Journal of molecular biology
2007
Corpus ID: 27130824
Highly Cited
2006
Highly Cited
2006
Biosynthesis of wybutosine, a hyper‐modified nucleoside in eukaryotic phenylalanine tRNA
A. Noma
,
Y. Kirino
,
Y. Ikeuchi
,
Tsutomu Suzuki
The EMBO journal
2006
Corpus ID: 6444368
Wybutosine (yW) is a tricyclic nucleoside with a large side chain found at the 3′‐position adjacent to the anticodon of…
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