Results 61 to 70 of about 1,030,385 (293)

A Novel Peptide-Based SILAC Method to Identify the Posttranslational Modifications Provides Evidence for Unconventional Ubiquitination in the ER-Associated Degradation Pathway. [PDF]

open access: yes, 2013
The endoplasmic reticulum-associated degradation (ERAD) pathway is responsible for disposing misfolded proteins from the endoplasmic reticulum by inducing their ubiquitination and degradation.
Anania, Veronica   +4 more
core   +3 more sources

Serine Metabolism Regulates the Replicative Senescence of Human Dental Pulp Cells through Histone Methylation

open access: yesCurrent Issues in Molecular Biology
Tissue regeneration therapy based on human dental pulp cells (hDPCs) faces the distinct challenge of cellular senescence during massive expansion in vitro.
Shuhan Zhou, Jingyao Cui, Yu Shi
doaj   +1 more source

Molecular structure of a 5,10‐methylenetetrahydrofolate dehydrogenase from the silkworm Bombyx mori

open access: yesFEBS Open Bio, 2019
The enzyme 5,10‐methylenetetrahydrofolate dehydrogenase (MTHFD) is essential for the production of certain amino acids (glycine, serine, and methionine) and nucleic acids (thymidylate and purine).
Mohammad R. Haque   +5 more
doaj   +1 more source

The serine transporter SdaC prevents cell lysis upon glucose depletion in Escherichia coli

open access: yesMicrobiologyOpen, 2020
The amino acid serine plays diverse metabolic roles, yet bacteria actively degrade exogenously provided serine via deamination to pyruvate. Serine deamination is thought to be a detoxification mechanism due to the ability of serine to inhibit several ...
Michelle A. Kriner   +1 more
doaj   +1 more source

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

open access: yesFEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes   +3 more
wiley   +1 more source

Androgen receptor phosphorylation at serine 515 by Cdk1 predicts biochemical relapse in prostate cancer patients [PDF]

open access: yes, 2013
<br>Background:Prostate cancer cell growth is dependent upon androgen receptor (AR) activation, which is regulated by specific kinases. The aim of the current study is to establish if AR phosphorylation by Cdk1 or ERK1/2 is of prognostic ...
BV Kallakury   +40 more
core   +1 more source

Biosynthesis of food constituents: Amino acids: 2. The alanine-valine-leucine, serine-cysteine-glycine, and aromatic and heterocyclic amino acids groups - a review

open access: yesCzech Journal of Food Sciences, 2006
This review article gives a survey of principal pathways that lead to the biosynthesis of the proteinogenic amino acids of the alanine-valine-leucine group starting with pyruvic acid from the glycolytic pathway and serine-cysteine-glycine group starting ...
Jan Velíšek, Karel Cejpek
doaj   +1 more source

Insights Into the Known 13C Depletion of Methane—Contribution of the Kinetic Isotope Effects on the Serine Hydroxymethyltransferase Reaction

open access: yesFrontiers in Chemistry, 2022
We determined the kinetic isotope effect on the serine hydroxymethyltransferase reaction (SHMT), which provides important C1 metabolites that are essential for the biosynthesis of DNA bases, O-methyl groups of lignin and methane. An isotope effect on the
Gerd Gleixner
doaj   +1 more source

Structural insights into lacto‐N‐biose I recognition by a family 32 carbohydrate‐binding module from Bifidobacterium bifidum

open access: yesFEBS Letters, EarlyView.
Bifidobacterium bifidum establishes symbiosis with infants by metabolizing lacto‐N‐biose I (LNB) from human milk oligosaccharides (HMOs). The extracellular multidomain enzyme LnbB drives this process, releasing LNB via its catalytic glycoside hydrolase family 20 (GH20) lacto‐N‐biosidase domain.
Xinzhe Zhang   +5 more
wiley   +1 more source

PPM1D phosphatase, a target of p53 and RBM38 RNA-binding protein, inhibits p53 mRNA translation via dephosphorylation of RBM38. [PDF]

open access: yes, 2015
PPM1D phosphatase, also called wild-type p53-induced phosphatase 1, promotes tumor development by inactivating the p53 tumor suppressor pathway.
Chen, X, Xu, E, Zhang, J, Zhang, M
core   +2 more sources

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