Results 91 to 100 of about 171,782 (185)

THE ROLE OF ATP-DEPENDENT PROTEASE CLP IN TRANSITION FROM STATIONARY TO LAG PHASE OF ESCHERICHIA COLI. [PDF]

open access: yes, 2023
Batch culture of E. coli shows typical growth curve, which consist of three phases, lag, logarithmic, and stationary phases. The stationary phase cells, which transferred to fresh medium, start growing again.
保科 真樹
core  

A Novel IDO1/NE Dual Inhibitor, IMM‐H018 Prevents the Primary and Secondary Sepsis and Ameliorates the Kidney Injury Through Inhibiting the Cytokine Storm and Microthrombosis, and Reversing Immunosuppression

open access: yesAdvanced Science, Volume 13, Issue 55, 5 October 2026.
IMM‐H018, a dual IDO1/NE inhibitor, demonstrates potent therapeutic efficacy in sepsis by simultaneously targeting excessive inflammation and immune dysfunction. It prevents both primary and secondary sepsis through anti‐inflammatory, immune‐restoring, and renoprotective mechanisms, reducing organ damage, improving immune homeostasis, preserving kidney
Yi Zhou   +11 more
wiley   +1 more source

PEAR1 Promotes Glucose Metabolism Reprogramming in Sepsis‐Associated Acute Lung Injury via AARS1‐Mediated HIF‐1α Lactylation

open access: yesAdvanced Science, Volume 13, Issue 56, 9 October 2026.
This study revealed that a PEAR1/HIF‐1α/ glycolysis/lactate/H3K18la positive feedback loop in PMVECs that drives the development of S‐ALI. Mechanistically, PEAR1 mediates the binding of HIF‐1α to AARS1, leading to the lactylation of HIF‐1α, the primary lactylation site of which is K172.
Shuai Li   +15 more
wiley   +1 more source

Pathological Signal‐Responsive Nanoplatforms for Sepsis: Integrating Biomarker Sensing With Spatiotemporal Drug Delivery and Immunomodulation

open access: yesAdvanced Science, Volume 13, Issue 58, 19 October 2026.
Biomarker‐triggered nanoplatforms transform sepsis therapy by coupling pathological sensing with precision drug release. This review reveals how microenvironment‐responsive nanomedicines enable stage‐specific intervention, improve therapeutic efficacy, and minimize systemic toxicity, while highlighting emerging opportunities for AI‐assisted and ...
Yukun Liu   +7 more
wiley   +1 more source

Omi/HtrA2 Regulates a Mitochondria-Dependent Apoptotic Pathway in a Murine Model of Septic Encephalopathy

open access: yesCellular Physiology and Biochemistry, 2018
Background/Aims: the pathogenesis of sepsis-associated encephalopathy (SAE) is multifactorial, involving neurotransmitter alterations, inflammatory cytokines, oxidative damage, mitochondrial dysfunction, apoptosis, and other factors.
Pengfei Wang   +3 more
doaj   +1 more source

Clp P represents a unique family of serine proteases.

open access: yesJournal of Biological Chemistry, 1990
The amino acid sequence of Clp P, the proteolytic subunit of the ATP-dependent Clp protease of Escherichia coli, closely resembles a protein encoded by chloroplast DNA, which is well conserved between chloroplasts of different plant species. The homology extends over almost the full length of the sequences of both proteins and consists of approximately
M R, Maurizi   +3 more
openaire   +2 more sources

Autophagy-like induction by the overexpression of the chloroplast protease subunit CrClpP5 increases nickel tolerance in Chlamydomonas reinhardtii

open access: yesEcotoxicology and Environmental Safety
Heavy metals are toxic to living organisms even at trace levels and persist in the environment due to their non-degradability. Understanding the mechanisms of heavy metal response and adaptation is therefore crucial.
Danqiong Huang   +6 more
doaj   +1 more source

The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate.

open access: yesJournal of Biological Chemistry, 1990
The clpA gene, which codes for the ATP-binding subunit of the ATP-dependent Clp protease of Escherichia coli, has been sequenced. The coding region contains a single open reading frame for a protein of 758 amino acids; within the amino acid sequence are two consensus sequences for ATP-binding sites.
S, Gottesman, W P, Clark, M R, Maurizi
openaire   +2 more sources

Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli.

open access: yesJournal of Biological Chemistry, 1990
The ATP-dependent Clp protease of Escherichia coli contains two dissimilar components: the Clp A regulatory polypeptide, with two ATP binding sites and intrinsic ATPase activity, and the Clp P subunit, which contains the proteolytic active site. The DNA sequence of the clpP gene predicts a protein of 207 amino acids (Mr 21,679), which is in close ...
M R, Maurizi   +6 more
openaire   +2 more sources

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