Top Cited Papers (WoS Core)
亚硝基化 Top 10 高被引论文
按 WoS Core Collection 总被引次数排序，覆盖方法学、机制研究与疾病转化。每条论文提供 DOI 直链 + 摘要前 280 字 + 前 4 位作者。
#1277 引用
PEERJ · 2013 · Vol.1
Xu, Y; Shao, XJ; Wu, LY; Deng, NY; et al.
As one of the most important and universal posttranslational modifications (PTMs) of proteins, S-nitrosylation (SNO) plays crucial roles in a variety of biological processes, including the regulation of cellular dynamics and many signaling events. Knowledge of SNO sites in protei…
#2215 引用
PLOS ONE · 2010 · Vol.5 (6)
Xue, Y; Liu, ZX; Gao, XJ; Jin, CJ; et al.
As one of the most important and ubiquitous post-translational modifications (PTMs) of proteins, S-nitrosylation plays important roles in a variety of biological processes, including the regulation of cellular dynamics and plasticity. Identification of S-nitrosylated substrates w…
#3188 引用
MOLECULAR & CELLULAR PROTEOMICS · 2016 · Vol.15 (1) · p.1-11
Yang, J; Carroll, KS; Liebler, DC
Cysteine occupies a unique place in protein chemistry. The nucleophilic thiol group allows cysteine to undergo a broad range of redox modifications beyond classical thiol-disulfide redox equilibria, including S-sulfenylation (-SOH), S-sulfinylation (-SO2H), S-sulfonylation (-SO3H…
#4139 引用
MOLECULAR NEURODEGENERATION · 2011 · Vol.6
Meng, FJ; Yao, DD; Shi, Y; Kabakoff, J; et al.
Background: Accumulation of aberrant proteins to form Lewy bodies (LBs) is a hallmark of Parkinson's disease (PD). Ubiquitination-mediated degradation of aberrant, misfolded proteins is critical for maintaining normal cell function. Emerging evidence suggests that oxidative/nitro…
#5139 引用
MOLECULAR NEURODEGENERATION · 2011 · Vol.6
Meng, FJ; Yao, DD; Shi, Y; Kabakoff, J; et al.
Background: Accumulation of aberrant proteins to form Lewy bodies (LBs) is a hallmark of Parkinson's disease (PD). Ubiquitination-mediated degradation of aberrant, misfolded proteins is critical for maintaining normal cell function. Emerging evidence suggests that oxidative/nitro…
#6133 引用
PROTEOMICS · 2007 · Vol.7 (17) · p.3066-3084
Lefievre, L; Chen, Y; Conner, SJ; Scott, JL; et al.
Nitric oxide (NO) enhances human sperm motility and capacitation associated with increased protein phosphorylation. NO activates soluble guanylyl cyclase, but can also modify protein function covalently via S-nitrosylation of cysteine. Remarkably, this mechanism remains unexplore…
#7109 引用
ONCOTARGET · 2017 · Vol.8 (8) · p.13338-13343
Liu, B; Wu, H; Zhang, DY; Wang, XL; et al.
To expedite the pace in conducting genome/proteome analysis, we have developed a Python package called Pse-Analysis. The powerful package can automatically complete the following five procedures: (1) sample feature extraction, (2) optimal parameter selection, (3) model training, …
#891 引用
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES · 2014 · Vol.15 (6) · p.10410-10423
Jia, CZ; Lin, X; Wang, ZP
Protein S-nitrosylation is a reversible post-translational modification by covalent modification on the thiol group of cysteine residues by nitric oxide. Growing evidence shows that protein S-nitrosylation plays an important role in normal cellular function as well as in various …
#986 引用
CANCER LETTERS · 2012 · Vol.320 (2) · p.123-129
Wang, ZQ
Protein S-nitrosylation is a covalent post-translational modification through coupling of a nitric oxide (NO) moiety with the reactive thiol group of a protein cysteine residue to form an S-nitrosothiol (SNO). S-nitrosylation is a key mechanism in the transmission of NO-based cel…
#1084 引用
PROTEOMICS · 2014 · Vol.14 (6) · p.750-762
Liu, P; Zhang, HM; Wang, H; Xia, YJ
Cellular redox status plays a key role in mediating various physiological and developmental processes often through modulating activities of redox-sensitive proteins. Various stresses trigger over-production of reactive oxygen/nitrogen species which lead to oxidative modification…