Ask about this productRelated genes to: DCTD antibody
- Gene:
- DCTD NIH gene
- Name:
- dCMP deaminase
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 4q35.1
- Locus Type:
- gene with protein product
- Date approved:
- 1995-10-02
- Date modifiied:
- 2014-11-19
Related products to: DCTD antibody
Related articles to: DCTD antibody
- We introduce a novel automated well plate sampling system (AmbiSampler) using laser ablation-rapid evaporative ionization mass spectrometry (LA-REIMS) for label-free high-throughput biochemical screening for small volume biological fluid samples and cell line panels from multiwell plates. The human blood serum samples featured intensive signals in the low m/z range including fatty acids and metabolites and in the higher (m/z > 600) range associated with complex lipids, peptides, and proteins. We demonstrate the current quantification performance of the system through blood serum samples spiked with labelled amino acid mix. Cell line analysis was demonstrated by analyzing the NCI60 human cell lines panel grown in multiwell plates. Without any sample preparation, these experiments yielded rich metabolic and lipidomic mass spectrometry profiles, with classification results showing a 98.7% correct classification rate. We demonstrated that the new high-throughput setup using LA-REIMS technology provides an efficient and versatile approach for ambient ionization mass spectrometric analysis of various biological samples in a high-throughput manner. - Source: PubMed
Publication date: 2026/04/28
Horkovics-Kováts Gabriel SSimon DanielSchäffer RichárdPap IstvánNozari ZahraKönig AlexanderDecking-Paede SonjaSzand RolandMolnár AdriennSchlosser GittaKucsma NóraSzakács GergelyTakáts ZoltánBalog Júlia - - Source: PubMed
Publication date: 2026/04/28
Ettedgui JessicaBlackman BurchelleRaju NatarajanKotler Samuel AChekmenev Eduard YGoodson Boyd MMerkle HellmutWoodroofe Carolyn CLeClair Christopher AKrishna Murali CSwenson Rolf E - Dr. C. Norman Coleman's impact is difficult to measure overall, even if one focuses only on his work as NCI's Radiation Research Program (RRP) leader. His laboratory work spanned immune-oncology and radiation therapy, RNA biology, normal tissue and tumor tissue radiobiology, and the development of tissue chips for use in radiation biology research. His programmatic leadership helped the RRP develop health equity programs addressing Native American access to optimal cancer care, evaluation of hadron therapy biology, radiation biology, reproducibility and rigor, foundational molecular biology of the tumor and normal tissue caused by radiation therapy dynamically, and global health and security issues. While doing all these things, he found time to mentor countless people in the field, many now leaders, and to read and discuss science across disciplines. He was a dedicated, caring, kind scientist who truly wanted to help and improve the world for others. - Source: PubMed
Publication date: 2026/03/24
Aryankalayil Molykutty JPrasanna Pataji G SBuchsbaum Jeffrey C - - Source: PubMed
Publication date: 2026/01/29
Zhong YuanpingZhang ChaoLi YuanChen DongqinTang ChunchunZheng XueZhu Zhaoqiong - Uridine monophosphate (UMP) is an essential nucleotide for infant formula, drug precursors, and DNA synthesis, yet current production methods face challenging downstream purification. Here, we established an efficient biocatalytic system for direct cytidine monophosphate (CMP)-to-UMP conversion using the deoxycytidine monophosphate deaminase (DCTD) from Enterobacteriaceae phage PG7, naturally active toward CMP. Evolutionary Scale Modeling-guided surface mutations combined with high-throughput screening generated the L99I variant, enhancing catalytic efficiency by 50-fold. Subsequent optimization through ProteinMPNN-guided design and ancestral sequence reconstruction produced the L99I/I92K double mutant, exhibiting 8-fold improved thermal stability and a total turnover number of 122,000. Molecular dynamics simulations elucidated the structural basis of the enhanced activity and stability. Using this optimal variant, 500 mM CMP was completely converted to UMP in 3 h with 99% yield. This study demonstrates a practical, green strategy for UMP production and highlights how rational enzyme engineering informed by allosteric insights can simultaneously improve catalytic efficiency, substrate specificity, and industrial applicability. - Source: PubMed
Publication date: 2025/11/06
Li Zong-LinChen TingLi Zhi-Min