Results 101 to 110 of about 43,191 (287)

Human Proteomic Variation Revealed by Combining RNA-Seq Proteogenomics and Global Post-Translational Modification (G-PTM) Search Strategy [PDF]

Journal of Proteome Research, 2016
Mass-spectrometry-based proteomic analysis underestimates proteomic variation due to the absence of variant peptides and posttranslational modifications (PTMs) from standard protein databases. Each individual carries thousands of missense mutations that lead to single amino acid variants, but these are missed because they are absent from generic ...
Cesnik, Anthony J., Shortreed, Michael R., Sheynkman, Gloria M., Frey, Brian L., Smith, Lloyd M.   +4 more
openaire   +2 more sources

PSMA8‐Containing 20S Proteasome Regulates Spermiogenesis and Male Fertility

Advanced Science, EarlyView.
PSMA8 assembles s20S proteasome that degrades specific substrates in elongating spermatids. Degradation of s20S‐substrates activates translation of FXR1‐target mRNAs, which are essential for mitochondrial sheath formation and sperm morphogenesis.
Huiwen Cao, Qianting Zhang, Wei Xu, Anxuan Fang, Haomang Xu, Cheng Qiu, Lugeng He, Chao Yu   +7 more
wiley   +1 more source

ProteomeScout: A repository and analysis resource for post-translational modifications and proteins [PDF]

, 2014
ProteomeScout (https://proteomescout.wustl.edu) is a resource for the study of proteins and their post-translational modifications (PTMs) consisting of a database of PTMs, a repository for experimental data, an analysis suite for PTM experiments, and a ...
Alex S. Holehouse, Barrett, Benjamini, Benson, Binns, Cock, Craveur, Dinkel, Finn, Fujita, Gnad, Griss, Guo, Gupta, Hornbeck, Hsu, Iwai, Joughin, Karolchik, Kristen M. Naegle, Lu, Matthew K. Matlock, Minguez, Moore, Naegle, Naegle, Naegle, NCBI Resource Coordinators, Obenauer, Prasad, Rose, Schmelzle, Sherry, Stockinger, Su, The Gene Ontology Consortium, The UniProt Consortium, Villaveces, Wagner, Walt, Wein, Witze, Wolf-Yadlin   +42 more
core   +3 more sources

Integrating Spatial Proteogenomics in Cancer Research

Advanced Science, EarlyView.
Xx xx. ABSTRACT Background: Spatial proteogenomics marks a paradigm shift in oncology by integrating molecular analysis with spatial information from both spatial proteomics and other data modalities (e.g., spatial transcriptomics), thereby unveiling tumor heterogeneity and dynamic changes in the microenvironment.
Yida Wang, Yang Wu, Feng Zhang, Parthiban Periasamy, Haiyue You, Denise Goh, Rachel Elizabeth Ann Fincham, Xin Ning, Danping Wu, Lu Liu, Ying Jiang, Zhiwen Qian, Joe Yeong, Yan Zhang   +13 more
wiley   +1 more source

Transcription factor LSF facilitiates lysine methylation of α-tubulin by microtubule-associated SET8 [PDF]

, 2019
Microtubules are critical for mitosis, cell motility, and protein and organelle transport, and are a validated target for anticancer drugs. However, tubulin regulation and recruitment in these cellular processes is less understood.
Chin, Hang Gyeong, Estève, Pierre Olivier, Hansen, Ulla, Lee, Jiyoung, Pradhan, Sriharsa, Ruse, Cristian, Schaus, Scott   +6 more
core   +1 more source

POU2F1 Promotes Chemoresistance in Colorectal Cancer Cells via Attenuates the MDR2 Degradation Mediated by PPP1R11 Lactylation

Advanced Science, EarlyView.
Schematic diagram of our study showing that highly expressed POU2F1 in colorectal cancer (CRC) can directly accelerate the cytosolic lactate export to decrease PPP1R11 lactylation at K59, thereby attenuating the E3 ligase enzyme activity and protein stability of PPP1R11, which inhibits the ubiquitination of MDR2 at K413 and K538 but increases the ...
Longzheng Xia, Jinguan Lin, Xianjie Jiang, Linda Oyang, Shiming Tan, Zongyao Ren, Qiu Peng, Qianjin Liao, Yujuan Zhou   +8 more
wiley   +1 more source

MAPping out distribution routes for kinesin couriers [PDF]

, 2013
In the crowded environment of eukaryotic cells, diffusion is an inefficient distribution mechanism for cellular components. Long-distance active transport is required and is performed by molecular motors including kinesins.
*Ackmann, Adams, Akhmanova, Akhmanova, Akiyama, Al-Bassam, Amadoro, Amos, Audebert, Baas, Baas, Bai, Bananis, Barlan, Bechstedt, Bieling, Binder, Black, Bobinnec, Bonnet, Boucher, Bouquet, Boyne, Bulinski, Bulinski, Burbridge, Burgess, Byrd, Cai, Charalambous, Chu, Cierpicki, Congdon, Cook, Corbo, De Vos, des Portes, des Portes, Desai, Deshpande, Deuel, Dijkmans, Dimitrov, DiTella, Dixit, Douglas, Drewes, Drewes, Duan, Dubey, Duff, Dunn, Eastwood, Ebneth, Erck, Faire, Fourniol, Francis, Friocourt, Fu, Fukushima, Fung, Galaburda, Garnham, Gleeson, Gleeson, Goldstein, Guillaud, Gurland, Hagiwara, Hammond, Hanger, Hanlon, Harada, Hardy, Heins, Hepp, Hidaka, Hirokawa, Hirokawa, Hoang, Horesh, Horiguchi, Huang, Hyman, Iijima, Ikegami, Ikegami, Iqbal, Iqbal, Ittner, Jacobson, Janke, Jenkins, Jimenez-Mateos, Ju, Kamal, Kanaan, Kanai, Kappeler, Kar, Kaslow, Kawaguchi, Kayadjanian, Khatoon, Khawaja, Kim, Klebe, Koizumi, Kondo, Konishi, Kosik, Kowall, Kreitzer, Kueh, LaPointe, Larcher, Larkin, Lawrence, Lazarov, Lee, Leger, Lewis, Liao, Lin, Liu, Liu, Liu, Liu, Lopez, Maas, Makrides, Mandelkow, Mandelkow, Mandell, Marcos, Marszalek, Massinen, Massow, Maurer, McVicker, Meng, Metzger, Miki, Miki, Mok, Moores, Moores, Morfini, Muresan, Nadar, Nakata, Nakata, Nakata, Navone, Nguyen, Nishimura, Noda, Noda, Nogales, Nosten-Bertrand, Omori, Pagon, Palazzo, Paturle-Lafanechere, Peck, Perez, Peterman, Pettersen, Pfenninger, Pfister, Polydoro, Reed, Reifert, Reiner, Saito, Santarella, Sapir, Saragoni, Schaar, Seidel, Seitz, Setou, Setou, Sharp, Shirasu, Silverman, Sindelar, Small, Song, Soppina, Sossey-Alaoui, Spiliotis, Spronsen, Stamer, Stokin, Stoothoff, Sung, Takei, Takemura, Tapia, Taylor, Teng, Terwel, Thinakaran, Thorn, Tien, Tilney, Tint, Tischfield, Trinczek, Tsai, Uchida, Utton, Vale, Vale, Verhey, Verhey, Vershinin, Vreugdenhil, Wade, Wagner, Walter, Wordeman, Xu, Yajima, Yamazaki, Yang, Yang, Ye, Yonekawa, Yoshimura, Yu, Yuan, Zempel, Zhang   +235 more
core   +1 more source

Sustainable Phosphorylated Cellulose Nanocrystals: A Dual‐Affinity Platform for High‐Efficiency Enrichment of Intact Glycopeptides and Phosphopeptides

Advanced Science, EarlyView.
AAA ABSTRACT Protein glycosylation and phosphorylation are critical post‐translational modifications (PTMs) governing nearly all cellular functions, yet their analysis remains challenging due to reliance on costly and unsustainable enrichment materials.
Jiaying Li, Wuming Fan, Xuyang Yue, Dongdong Wang, Xiangyu Tang, Zhuo Zhang, Yonggui Wang, Yanjun Xie, Mingliang Ye, Hongqiang Qin   +9 more
wiley   +1 more source

Proteomic Analysis of Histone Variants and Their PTMs: Strategies and Pitfalls

Proteomes, 2018
Epigenetic modifications contribute to the determination of cell fate and differentiation. The molecular mechanisms underlying histone variants and post-translational modifications (PTMs) have been studied in the contexts of development, differentiation,
Sara El Kennani, Marion Crespo, Jérôme Govin, Delphine Pflieger   +3 more
doaj   +1 more source

Kinsenoside Targets IDH1 to Restore Microglial Immune‐Metabolic Homeostasis for Alzheimer's Disease Therapy

Advanced Science, EarlyView.
Dysregulated TCA cycle contributes to Alzheimer's disease (AD) pathogenesis. Here, we show that microglial isocitrate dehydrogenase 1 (IDH1) is a critical driver. Elevated IDH1 disrupts citrate metabolism and mitochondrial function, exacerbating AD pathology.
Qianqian Li, Yajin Liao, Yan‐bo Zhao, Hongxing Wu, Tong Jin, Shuoshuo Li, Yuhan Liu, Peng Li, Songying Ouyang, Zekai Li, YuTing Xia, Qian Hua, Rui‐Yuan Pan, Zengqiang Yuan   +13 more
wiley   +1 more source