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Refinado por: Nome da Publicação: The Journal Of Biological Chemistry remover
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11
eIF5 stimulates the CUG initiation of RAN translation of poly-GA dipeptide repeat protein (DPR) in C9orf72 FTLD/ALS
eIF5 stimulates the CUG initiation of RAN translation of poly-GA dipeptide repeat protein (DPR) in C9orf72 FTLD/ALS
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eIF5 stimulates the CUG initiation of RAN translation of poly-GA dipeptide repeat protein (DPR) in C9orf72 FTLD/ALS

Gotoh, Shiho ; Mori, Kohji ; Fujino, Yuzo ; Kawabe, Yuya ; Yamashita, Tomoko ; Omi, Tsubasa ; Nagata, Kenichi ; Tagami, Shinji ; Nagai, Yoshitaka ; Ikeda, Manabu

The Journal of biological chemistry, 2024-03, Vol.300 (3), p.105703-105703, Article 105703 [Periódico revisado por pares]

United States: Elsevier Inc

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12
LncRNA CHROMR/miR-27b-3p/MET axis promotes the proliferation, invasion, and contributes to rituximab resistance in diffuse large B-cell lymphoma
LncRNA CHROMR/miR-27b-3p/MET axis promotes the proliferation, invasion, and contributes to rituximab resistance in diffuse large B-cell lymphoma
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LncRNA CHROMR/miR-27b-3p/MET axis promotes the proliferation, invasion, and contributes to rituximab resistance in diffuse large B-cell lymphoma

Liu, Chang ; Zhao, Xinan ; Wang, Zifeng ; Zhang, Chan ; Zheng, Wenbin ; Zhu, Xiaoxia ; Zhang, Dong ; Gong, Tao ; Zhao, Hong ; Li, Feng ; Guan, Tao ; Guo, Xiangyang ; Zhang, Hongwei ; Yu, Baofeng

The Journal of biological chemistry, 2024-03, Vol.300 (3), p.105762-105762, Article 105762 [Periódico revisado por pares]

United States: Elsevier Inc

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13
Satellite double-stranded RNA induces mesenchymal transition in pancreatic cancer by regulating alternative splicing
Satellite double-stranded RNA induces mesenchymal transition in pancreatic cancer by regulating alternative splicing
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Satellite double-stranded RNA induces mesenchymal transition in pancreatic cancer by regulating alternative splicing

Iwata, Takuma ; Kishikawa, Takahiro ; Seimiya, Takahiro ; Notoya, Genso ; Suzuki, Tatsunori ; Shibata, Chikako ; Miyakawa, Yu ; Odawara, Nariaki ; Funato, Kazuyoshi ; Tanaka, Eri ; Yamagami, Mari ; Sekiba, Kazuma ; Otsuka, Motoyuki ; Koike, Kazuhiko ; Fujishiro, Mitsuhiro

The Journal of biological chemistry, 2024-03, Vol.300 (3), p.105742-105742, Article 105742 [Periódico revisado por pares]

United States: Elsevier Inc

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14
Large-scale column-free purification of bovine F-ATP synthase
Large-scale column-free purification of bovine F-ATP synthase
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Large-scale column-free purification of bovine F-ATP synthase

Jiko, Chimari ; Morimoto, Yukio ; Tsukihara, Tomitake ; Gerle, Christoph

The Journal of biological chemistry, 2024-02, Vol.300 (2), p.105603-105603, Article 105603 [Periódico revisado por pares]

United States: Elsevier Inc

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15
The dual GGDEF/EAL domain enzyme PA0285 is a Pseudomonas species housekeeping phosphodiesterase regulating early attachment and biofilm architecture
The dual GGDEF/EAL domain enzyme PA0285 is a Pseudomonas species housekeeping phosphodiesterase regulating early attachment and biofilm architecture
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The dual GGDEF/EAL domain enzyme PA0285 is a Pseudomonas species housekeeping phosphodiesterase regulating early attachment and biofilm architecture

Eilers, Kira ; Hoong Yam, Joey Kuok ; Liu, Xianghui ; Goh, Yu Fen ; To, Ka-Ning ; Paracuellos, Patricia ; Morton, Richard ; Brizuela, Jaime ; Hui Yong, Adeline Mei ; Givskov, Michael ; Freibert, Sven-Andreas ; Bange, Gert ; Rice, Scott A. ; Steinchen, Wieland ; Filloux, Alain

The Journal of biological chemistry, 2024-02, Vol.300 (2), p.105659-105659, Article 105659 [Periódico revisado por pares]

United States: Elsevier Inc

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16
Clostridioides difficile canonical L,D-transpeptidases catalyze a novel type of peptidoglycan cross-links and are not required for beta-lactam resistance
Clostridioides difficile canonical L,D-transpeptidases catalyze a novel type of peptidoglycan cross-links and are not required for beta-lactam resistance
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Clostridioides difficile canonical L,D-transpeptidases catalyze a novel type of peptidoglycan cross-links and are not required for beta-lactam resistance

Galley, Nicola F ; Greetham, Darren ; Alamán-Zárate, Marcel G ; Williamson, Mike P ; Evans, Caroline A ; Spittal, William D ; Buddle, Jessica E ; Freeman, Jane ; Davis, Georgina L ; Dickman, Mark J ; Wilcox, Mark H ; Lovering, Andrew L ; Fagan, Robert P ; Mesnage, Stéphane

The Journal of biological chemistry, 2024-01, Vol.300 (1), p.105529-105529, Article 105529 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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17
Specific protonation of acidic residues confers K + selectivity to the gastric proton pump
Specific protonation of acidic residues confers K + selectivity to the gastric proton pump
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Specific protonation of acidic residues confers K + selectivity to the gastric proton pump

Madapally, Hridya Valia ; Abe, Kazuhiro ; Dubey, Vikas ; Khandelia, Himanshu

The Journal of biological chemistry, 2024-01, Vol.300 (1), p.105542-105542, Article 105542 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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18
Ubiquitin ligase NEDD4 promotes the proliferation of hepatocellular carcinoma cells through targeting PCDH17 protein for ubiquitination and degradation
Ubiquitin ligase NEDD4 promotes the proliferation of hepatocellular carcinoma cells through targeting PCDH17 protein for ubiquitination and degradation
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Ubiquitin ligase NEDD4 promotes the proliferation of hepatocellular carcinoma cells through targeting PCDH17 protein for ubiquitination and degradation

Liu, Zhiyi ; Hu, Qinghe ; Hu, Bin ; Cao, Kuan ; Xu, Tao ; Hou, Tianqi ; Cao, Tong ; Wang, Renhao ; Shi, Hengliang ; Zhang, Bin

The Journal of biological chemistry, 2024-01, Vol.300 (1), p.105593-105593, Article 105593 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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19
Protocatechuate hydroxylase is a novel group A flavoprotein monooxygenase with a unique substrate recognition mechanism
Protocatechuate hydroxylase is a novel group A flavoprotein monooxygenase with a unique substrate recognition mechanism
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Protocatechuate hydroxylase is a novel group A flavoprotein monooxygenase with a unique substrate recognition mechanism

Katsuki, Nozomi ; Fukushima, Riku ; Doi, Yuki ; Masuo, Shunsuke ; Arakawa, Takatoshi ; Yamada, Chihaya ; Fushinobu, Shinya ; Takaya, Naoki

The Journal of biological chemistry, 2024-01, Vol.300 (1), p.105508-105508, Article 105508 [Periódico revisado por pares]

United States

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20
Structural and functional studies reveal the molecular basis of substrate promiscuity of a glycosyltransferase originating from a major agricultural pest
Structural and functional studies reveal the molecular basis of substrate promiscuity of a glycosyltransferase originating from a major agricultural pest
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Structural and functional studies reveal the molecular basis of substrate promiscuity of a glycosyltransferase originating from a major agricultural pest

Arriaza, Ricardo Hernandez ; Abiskaroon, Brendan ; Patel, Megha ; Daneshian, Leily ; Kluza, Anna ; Snoeck, Simon ; Watkins, Maxwell B. ; Hopkins, Jesse B. ; Van Leeuwen, Thomas ; Grbic, Miodrag ; Grbic, Vojislava ; Borowski, Tomasz ; Chruszcz, Maksymilian

The Journal of biological chemistry, 2023-12, Vol.299 (12), p.105421-105421, Article 105421 [Periódico revisado por pares]

United States: Elsevier Inc

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