Conditional essentiality of the 11-subunit complex I-like enzyme in strict anaerobes: the case of strain DCB-2.

In oxidative phosphorylation, respiratory complex I serves as an entry point in the electron transport chain for electrons generated in catabolic processes in the form of NADH. An ancestral version of the complex, lacking the NADH-oxidising module, is encoded in a significant number of bacterial genomes. Amongst them is , a strict anaerobe capable of conserving energy via organohalide respiration.

Phosphoproteomics and morphology of stored human red blood cells treated by protein tyrosine phosphatases inhibitor.

The process of protein phosphorylation is involved in numerous cell functions. In particular, phosphotyrosine (pY) has been reported to play a role in red blood cell (RBC) functions, including the cytoskeleton organization. During their storage before transfusion, RBCs suffer from storage lesions that affect their energy metabolism and morphology.

Resistance mechanism to Notch inhibition and combination therapy in human T-cell acute lymphoblastic leukemia.

Gain-of-function mutations in NOTCH1 are among the most frequent genetic alterations in T-cell acute lymphoblastic leukemia (T-ALL), highlighting the Notch signaling pathway as a promising therapeutic target for personalized medicine. Yet, a major limitation for long-term success of targeted therapy is relapse due to tumor heterogeneity or acquired resistance. Thus, we performed a genome-wide CRISPR-Cas9 screen to identify prospective resistance mechanisms to pharmacological NOTCH inhibitors and novel targeted combination therapies to efficiently combat T-ALL.

Proteome adaptations of the organohalide-respiring strain DCB-2 to various energy metabolisms.

Introduction: was isolated for its ability to use organohalogens as terminal electron acceptors organohalide respiration (OHR). In contrast to obligate OHR bacteria, spp. show a highly versatile energy metabolism with the capacity to use different electron donors and acceptors and to grow fermentatively.