Results 51 to 60 of about 34,064 (250)

Nephrotoxic Action of Spermine

open access: yesExperimental Biology and Medicine, 1952
ConclusionsSpermine administered parenterally is highly active in producing renal injury in mice, rats, and rabbits. This property was not observed for spermidine, putrescine, or cadaverine.
S M, ROSENTHAL   +2 more
openaire   +2 more sources

Spermine induces cataract and 43-kDa protein that binds spermine possibly participates in the cataract formation

open access: yes, 2003
Among polyamines (putrescine, spermidine, and spermine), spermine specifically induces cataract in an organ cultured lens. Spermine uptake nearly paralleled the cataract formation.
Kunio Nakashima   +9 more
core   +1 more source

Upadacitinib Restrains the Pathogenic Fitness of CD4+ T Cells and Aberrant B Cell Programming in Optic Neuritis

open access: yesAdvanced Science, EarlyView.
Single‐cell profiling and functional perturbation reveal coordinated JAK1‐pSTAT3 downstream programs in optic neuritis, including MCL1‐dependent fitness of pathogenic CD4+ Tem cells and glycolysis‐linked, cholesterol‐sensitive B‐cell responses associated with RORA. Upadacitinib disrupts this reciprocal T‐B‐cell circuit and alleviates neuroinflammation,
Gengchen Jiang   +12 more
wiley   +1 more source

Transcriptomic data for analyzing global gene expression patterns in Methicillin-resistance Staphylococcus aureus in response to spermine and oxacillin stress

open access: yesData in Brief, 2018
Methicillin-resistant Staphylococcus aureus (MRSA) is a rapidly emerging bacteria causing infection, which has developed resistance to most of the beta-lactam antibiotics because of newly acquired low-affinity penicillin binding protein (PBP2a), which ...
Shrikant Pawar, Xiangyu Yao, ChungDar Lu
doaj   +1 more source

Structure and transport mechanism of P5B-ATPases

open access: yesNature Communications, 2021
In human cells, P5B‐ATPases execute export of spermine from lysosomes to the cytosol, but the mechanisms of spermine recognition, uptake and transport remain elusive. Here the authors present cryo‐EM structures of a yeast homolog of human ATP13A2‐5, Ypk9,
Ping Li   +4 more
doaj   +1 more source

Lack of Influence of Spermine or Diet on Calf Spermine Oxidase Formation

open access: yesJournal of Dairy Science, 1965
Abstract Studies were conducted to ascertain the changes in blood plasma spermine oxidase activity in the young dairy calf as the animal developed. Results show that there is a steady increase in plasma spermine oxidase activity up until 40-60 days of age with no further increase.
E, UEYAMA, C L, DAVIS, M J, WOLIN
openaire   +2 more sources

Design of a Novel Diamine Biosensor to Guide the Engineering of Escherichia coli for Cadaverine Overproduction

open access: yesAdvanced Science, EarlyView.
A high‐throughput screening platform was established by integrating an in vivo cadaverine biosensor with a fluorescence‐activated cell sorting (FACS) system. Biosensor‐driven specific exporter tuning, pathway optimization and genome‐wide target mining were conducted to maximize cadaverine production in Escherichia coli.
Jia Feng   +13 more
wiley   +1 more source

Spermine

open access: yes, 2002
Inelastic Neutron Scattering spectrum of Spermine, H₂N(CH₂)₃NH(CH₂)₄NH(CH₂)₃NH₂, measured on the TOSCA ...
M. P. M. Marques, Universidade de Coimbra, Portugal
core   +1 more source

On the mechanism of spermine transport in liver mitochondria [PDF]

open access: yes, 1988
Spermine penetrates the mitochondrial matrix at significant rates which increase sharply and non-ohmically with membrane potential. In this respect, spermine uptake is qualitatively similar to that of other cations whose electrophoretic transport has ...
Siliprandi N   +9 more
core   +1 more source

SAT1‐Induced Spermidine Depletion Potentiates Food Allergy

open access: yesAdvanced Science, EarlyView.
Spermidine depletion, driven by upregulated spermidine/spermine N1‐acetyltransferase (SAT1), potentiates food allergy by promoting mast cell degranulation through autophagy suppression. SAT1 physically interacts with the long noncoding RNA Cdk19os to inhibit Atg5 and Atg7, disrupting autophagic flux.
Manman Liu   +8 more
wiley   +1 more source

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