Results 141 to 150 of about 1,958,325 (325)

Key Regulators of Parasite Biology Viewed Through a Post‐Translational Modification Repertoire

open access: yesPROTEOMICS, EarlyView.
ABSTRACT Parasites are the leading causes of morbidity and mortality in both humans and animals, imposing substantial socioeconomic burdens worldwide. Controlling parasitic diseases has become one of the key issues in achieving “One Health”. Most parasites have sophisticated life cycles exhibiting progressive developmental stages, morphologies, and ...
Naiwen Zhang, Ning Jiang, Qijun Chen
wiley   +1 more source

Real estate in the DNA damage response: Ubiquitin and SUMO ligases home in on DNA double-strand breaks

open access: yesFrontiers in Genetics, 2016
Ubiquitin and the ubiquitin-like modifier SUMO are intimately connected with the cellular response to various types of DNA damage. A striking feature is the local accumulation of these proteinaceous post-translational modifications in the direct vicinity
Nico P. Dantuma, Annika ePfeiffer
doaj   +1 more source

Proteome Analysis of Corynebacterium diphtheriae–Macrophage Interaction

open access: yesPROTEOMICS, EarlyView.
ABSTRACT Contact of Corynebacterium diphtheriae with macrophages induces adaptations on both bacterial and cellular sides. The study presented here was aiming to shed light on the simultaneous intracellular adaptation of the bacteria and changes in the proteome of the phagocytes in response to the internalization of C. diphtheriae.
Luca Musella   +6 more
wiley   +1 more source

Role of Desumoylation in the Development of Prostate Cancer

open access: yesNeoplasia: An International Journal for Oncology Research, 2006
SUMO is a novel ubiquitin-like protein that can covalently modify a large number of nuclear proteins. SUMO modification has emerged as an important regulatory mechanism for protein function and localization.
Jinke Cheng   +4 more
doaj   +1 more source

Dissecting Distinct Roles of NEDDylation E1 Ligase Heterodimer APPBP1 and UBA3 Reveals Potential Evolution Process for Activation of Ubiquitin-related Pathways. [PDF]

open access: yes, 2018
Despite the similar enzyme cascade in the Ubiquitin and Ubiquitin-like peptide(Ubl) conjugation, the involvement of single or heterodimer E1 activating enzyme has been a mystery.
Gaieb, Zied   +7 more
core  

The ubiquitin E3/E4 ligase, UBE4A, fine-tunes protein ubiquitylation and accumulation at sites of DNA damage facilitating double-strand break repair [PDF]

open access: yes, 2018
Double-strand breaks (DSBs) are critical DNA lesions that robustly activate the elaborate DNA damage response (DDR) network. We identified a critical player in DDR fine-tuning - the E3/E4 ubiquitin ligase, UBE4A.
Baranes Bachar, Keren   +4 more
core   +1 more source

Chemical Tools and Biochemical Assays for SUMO Specific Proteases (SENPs)

open access: yesACS Chemical Biology, 2019
SUMOylation is a reversible and highly dynamic post-translational modification of target proteins by small ubiquitin-like modifiers (SUMO). It is orchestrated by SUMO-activating, -conjugating, and -ligating enzymes in a sequential manner and is important
Yuqing Jia   +3 more
semanticscholar   +1 more source

The SIRT1 N‐Terminal Domain as a Common Binding Interface for PPARγ Anchoring

open access: yesProteins: Structure, Function, and Bioinformatics, EarlyView.
ABSTRACT Insulin resistance, a global health threat linked to type 2 diabetes and obesity, can be addressed by modulating the activity of the Sirtuin 1 (SIRT1), a deacetylase that enhances insulin sensitivity by deacetylating the Peroxisome Proliferator‐Activated Receptor Gamma (PPARγ) at lysine 268 and 293. Understanding the binding interfaces between
Caique Camargo Malospirito   +7 more
wiley   +1 more source

Optimizing (Bio) Catalysis with Liquid‐Liquid Phase Separation Systems

open access: yesChemSystemsChem, EarlyView.
This review highlights how LLPS creates membraneless compartments involved in different scenarios in nature. It further explores different examples that focus on the development of synthetic coacervates that enhance catalytic efficiency by concentrating reactants, or by the direct influence of the coacervates building blocks themselves.
David Q. P. Reis   +4 more
wiley   +1 more source

Table S1 from T Cell–intrinsic Immunomodulatory Effects of TAK-981 (Subasumstat), a SUMO-activating Enzyme Inhibitor, in Chronic Lymphocytic Leukemia

open access: green, 2023
Vi Lam   +13 more
  +4 more sources

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