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The purinergic signaling interfaces in breast cancer angiogenesis. [PDF]
da Silva FC +3 more
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The 5' Cap Epitranscriptome and Beyond: Natural and Engineered 5' Cap Modifications for Optimizing mRNA Therapeutics and Functional Studies. [PDF]
Dahm GC +3 more
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TRPM2: a pivotal player in tumor progression and a promising therapeutic target. [PDF]
Chen Z, Wu Z, Xu T, Yu F, Wang D.
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Molecularly Targeted Cancer Medications and Kidney Health.
Ziolkowski S +9 more
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Synthesis of Well‐Defined Adenosine Diphosphate Ribose Oligomers
Angewandte Chemie International Edition, 2015AbstractThe post‐translational modification of proteins that is known as adenosine diphosphate ribosylation (ADPr) regulates a wide variety of important biological processes, such as DNA‐damage repair and cellular metabolism. This modification is also involved in carcinogenesis and the process of aging. Therefore, a better understanding of the function
Kistemaker, H.A.V. +5 more
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Synthesis of Simple Adenosine Diphosphate Ribose Analogues
Nucleosides, Nucleotides & Nucleic Acids, 2008[See figures]. The synthesis of analogues of adenosine diphosphate ribose and acetylated adenosine diphosphate ribose, modified at the northern pentose, is reported. The stereochemistry at the acetylated centers was chosen to minimize acetyl migration and dictated the overall synthetic strategy.
Chevallier, Olivier, Migaud, Marie
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ADENOSINE DIPHOSPHATE RIBOSE PYROPHOSPHOHYDROLASE IN HUMAN SKIN
The Journal of Dermatology, 1980ABSTRACTAdenosine diphosphate ribose (ADPR) pyrophosphohydrolase (ADPR‐PPase), which catalyzes the hydrolysis of ADPR to yield adenosine monophosphate (AMP) and ribose‐5′‐phosphate, was assayed in human penile foreskin. Since ADPR is formed from nicotinamide adenine dinucleotide (NAD) by NAD glycohydrolase (NADase), NADase was also assayed in human ...
Y P, Kim, J B, Kahng, J Y, Choi
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Isopolar Phosphonate Analogue of Adenosine Diphosphate Ribose
Organic Letters, 2004[structure: see text] The synthesis of the bisphosphonate ADP-ribose, in which acetylene has replaced the oxygen of the pyrophosphate linkage, is reported.
Migaud, Marie, Van Derpoorten, K.
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Biochemistry, 1976
An antibody has been prepared which is highly specific for poly(adenosine diphosphate-ribose). Neither poly(A), DNA, nor a variety of adenine-containing nucleosides or nucleotides were effective in competing with poly(ADP-ribose) for binding to the antibody. Of all compounds tested, only adenosine diphosphate-ribose competed for binding to the antibody.
W R, Kidwell, M G, Mage
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An antibody has been prepared which is highly specific for poly(adenosine diphosphate-ribose). Neither poly(A), DNA, nor a variety of adenine-containing nucleosides or nucleotides were effective in competing with poly(ADP-ribose) for binding to the antibody. Of all compounds tested, only adenosine diphosphate-ribose competed for binding to the antibody.
W R, Kidwell, M G, Mage
openaire +2 more sources

