Results 31 to 40 of about 1,007,835 (176)

Acetylation site specificities of lysine deacetylase inhibitors in human cells [PDF]

, 2015
This work was supported by the Hallas Møller Investigator grant from the Novo Nordisk Foundation to C.C. S.A.W. and P.B. were supported by individual postdoctoral grants from the Danish Research Council (FSS: 10-085134, FSS: 12-12610). C.C.
Sebastian A Wagner, Jensen, Lars J., Jensen, Lars J, Chunaram Choudhary, Qi, Yun, Sonia Lain, Wagner, Sebastian A, Weinert, Brian T., James E Bradner, McCarthy, Anna R, Mann, Matthias, Yasuyuki Miyake, Westwood, Nicholas J, Schölz, Christian, Wagner, Sebastian A., Choudhary, Chunaram, Choudhary, Chuna Ram, Matthias, Patrick, Bradner, James E, Anna R McCarthy, Werner Streicher, Weinert, Brian Tate, Lain, Sonia, Bradner, James E., Matthias Mann, Nicholas J Westwood, Lars J Jensen, Jürgen Cox, Westwood, Nicholas James, Brian T Weinert, Cox, Jürgen, Christian Schölz, Streicher, Werner, McCarthy, Anna Rose, Lain, Sonya, Beli, Petra, Qi, Jun, Petra Beli, Jun Qi, Miyake, Yasuyuki, Patrick Matthias   +40 more
core   +1 more source

Paclitaxel Enhances the Innate Immunity by Promoting NLRP3 Inflammasome Activation in Macrophages

Frontiers in Immunology, 2019
Microtubules play critical roles in regulating the activation of NLRP3 inflammasome and microtubule-destabilizing agents such as colchicine have been shown to suppress the activation of this inflammasome.
Qiong-zhen Zeng, Fan Yang, Chen-guang Li, Li-hui Xu, Xian-hui He, Feng-yi Mai, Chen-ying Zeng, Cheng-cheng Zhang, Qing-bing Zha, Dong-yun Ouyang   +9 more
doaj   +1 more source

Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro. [PDF]

PLoS ONE, 2012
Kinesin-1 plays a major role in anterograde transport of intracellular cargo along microtubules. Currently, there is an ongoing debate of whether α-tubulin K40 acetylation directly enhances the velocity of kinesin-1 and its affinity to the microtubule ...
Wilhelm J Walter, Václav Beránek, Elisabeth Fischermeier, Stefan Diez   +3 more
doaj   +1 more source

HDAC6 Inhibition Alleviates Ischemia- and Cisplatin-Induced Acute Kidney Injury by Promoting Autophagy

Cells, 2022
Histone deacetylase (HDAC) 6 exists exclusively in cytoplasm and deacetylates cytoplasmic proteins such as α-tubulin. HDAC6 dysfunction is associated with several pathological conditions in renal disorders, including UUO-induced fibrotic kidneys and ...
Lang Shi, Zhixia Song, Chenglong Li, Fangjing Deng, Yao Xia, Jing Huang, Xiongfei Wu, Jiefu Zhu   +7 more
doaj   +1 more source

Inhibitor of DNA binding 2 (Id2) mediates microtubule polymerization in the brain by regulating αK40 acetylation of α-tubulin

Cell Death Discovery, 2021
Acetylation of α-tubulin lysine 40 (αK40) contributes to microtubule (MT) stability and is essential for neuronal development and function, whereas excessive αK40 deacetylation is observed in neurodegenerative disorders including Alzheimer’s disease (AD).
Taegwan Yun, Hyo Rim Ko, Dong-Kyu Jo, Kye Won Park, Sung-Woo Cho, Jihoe Kim, Jee-Yin Ahn   +6 more
doaj   +1 more source

The loss of α- and β-tubulin proteins are a pathological hallmark of chronic alcohol consumption and natural brain ageing [PDF]

, 2018
Repetitive excessive alcohol intoxication leads to neuronal damage and brain shrinkage. We examined cytoskeletal protein expression in human post-mortem tissue from Brodmann’s area 9 of the prefrontal cortex (PFC).
Kusum K. Kharbanda, Johnson, Laura, Carter, Wayne G., Gerdes, Henry, Wajana L. Labisso, Jack Enticott, Labisso, Wajana L., Kocon, Artur, Enticott, Jack, Grzeskowiak, John, Tarbox, Rebecca, Osna, Natalia A., Allen, George, Kharbanda, Kusum, Wajana L. Labisso, Ana-Caroline Raulin, George Allen, Erdozain Fernández, Amaia Maite, Rebecca Tarbox, Wayne G. Carter, Lucky L. Nwidu, Luis F. Callado, Henry K. Gerdes, Callado, Luis, Fryni Drizou, Raulin, Ana-Caroline, Luis F. Callado, Natalia A. Osna, John Grzeskowiak, Osna, Natalia, Nwidu, Lucky, Henry K. Gerdes, Morentin Campillo, Benito, Natalia A. Osna, Wayne G. Carter, Lucky L. Nwidu, Artur Kocon, Benito Morentin, Amaia M. Erdozain, Declan Wayne, Erdozain, Amaia, Carter, Wayne, Daniela Schwendener, Schwendener, Daniela, Drizou, Fryni, Gerdes, Henry K., Labisso, Wajana, Amaia M. Erdozain, Kusum K. Kharbanda, Wayne, Declan, Laura Johnson, Kharbanda, Kusum K., Nwidu, Lucky L., Callado Hernando, Luis Felipe, Morentin, Benito   +54 more
core   +1 more source

Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation

, 2012
Protein acetylation is an important posttranslational modification with the recent identification of new substrates and enzymes, new links to disease, and modulators of protein acetylation for therapy.
Friedmann, David R, Nachury, Maxence V, Aguilar, Andrea, Marmorstein, Ronen, Fan, Jiayi   +4 more
core   +1 more source

Microtubule Acetylation Is Required for Mechanosensation in Drosophila

Cell Reports, 2018
Summary: At the cellular level, α-tubulin acetylation alters the structure of microtubules to render them mechanically resistant to compressive forces. How this biochemical property of microtubule acetylation relates to mechanosensation remains unknown ...
Connie Yan, Fei Wang, Yun Peng, Claire R. Williams, Brian Jenkins, Jill Wildonger, Hyeon-Jin Kim, Jonathan B. Perr, Joshua C. Vaughan, Megan E. Kern, Michael R. Falvo, E. Timothy O’Brien, III, Richard Superfine, John C. Tuthill, Yang Xiang, Stephen L. Rogers, Jay Z. Parrish   +16 more
doaj   +1 more source

Tubulin acetylation enhances lung cancer resistance to paclitaxel-induced cell death through Mcl-1 stabilization

Cell Death Discovery, 2021
The posttranslational modifications (PTMs) of microtubules have been reported to play an important role in cancer aggressiveness, including apoptosis resistance.
Onsurang Wattanathamsan, Rawikorn Thararattanobon, Ratchanee Rodsiri, Pithi Chanvorachote, Chanida Vinayanuwattikun, Varisa Pongrakhananon   +5 more
doaj   +1 more source

The effect of PRRSV and HDAC6 overexpression on α-tubulin acetylation.

, 2017
Kinetic analysis of JXA1-induced α-tubulin acetylation in MARC-145 cells (A) and in untreated cells (B). Kinetic analysis of JXA1-induced α-tubulin acetylation in PAMs (C) and in untreated cells (D). Kinetic analysis of JXA1-induced α-tubulin acetylation
Tianyu Lu (3615449), Kegong Tian (30834), Lin Liu (74495), Zhiyuan Song (553541), Meng Wang (124646), Qiuyan Li (526038), Ning Li (45258), Zhiguo Li (431917)   +7 more
core   +1 more source