Results 61 to 70 of about 38,432 (164)

Insights into the renal pathophysiology in Hermansky‐Pudlak syndrome‐1 from urinary extracellular vesicle proteomics and a new mouse model

open access: yesFEBS Letters, Volume 599, Issue 7, Page 1055-1074, April 2025.
Hermansky‐Pudlak syndrome type 1 (HPS‐1) is a rare, autosomal recessive disorder with poorly understood renal involvement. Urinary extracellular vesicle (uEV) proteomics and a novel Hps1 mouse model reveal mitochondrial abnormalities and lipid accumulation in HPS‐1 kidney proximal tubule cells. Serum ApoA1 correlates with kidney function in our patient
Dawn M. Maynard   +7 more
wiley   +1 more source

Adenosine Triphosphatase Activities of Muscle Sarcolemma

open access: yesJournal of Biological Chemistry, 1973
Abstract Isolated sarcolemma hydrolyzed ATP in the presence of Mg2+ and Ca2+. MgATPase was stimulated by low concentrations of Ca2+ and inhibited by high concentrations of this cation. Membranes hydrolyzed p-nitrophenylphosphate in the presence of Mg2+; this activity was stimulated by Ca2+ and K+.
George I. Drummond   +2 more
openaire   +3 more sources

The Influence of Sodium Phenobarbital on the Hepatic Adenosine Triphosphatase Activity and the Development of this Enzyme in the Rat [PDF]

open access: yes, 1970
The purpose of this study was two-fold: {A) To obtain information concerning the influence of sodium phenobarbital on the hepatic microsomal enzyme system which reduces adenosine triphosphate in adult male and female rats; (B) To measure the development ...
Mettler, Gerald H.
core   +1 more source

36 degree step size of proton-driven c-ring rotation in FoF1-ATP synthase [PDF]

open access: yes, 2009
Synthesis of the biological "energy currency molecule" adenosine triphosphate ATP is accomplished by FoF1-ATP synthase. In the plasma membrane of Escherichia coli, proton-driven rotation of a ring of 10 c subunits in the Fo motor powers catalysis in the ...
Boersch, Michael   +6 more
core   +2 more sources

ADENOSINE TRIPHOSPHATASE: A NEUROHISTOCHEMICAL STUDY [PDF]

open access: yesJournal of Histochemistry & Cytochemistry, 1962
The location of adenosine triphosphatase in the brain has been studied in rapidly frozen-dried cerebral tissues of the Wistar rat. It is found that adenosine triphosphatase is an almost exclusively nuclear enzyme. Two tissue fractions of the cerebrum were separated, so that one sample was made up of vascular elements, and the other of neural ...
openaire   +2 more sources

Histochemical Studies on the Nervous and Humoral Regulation of Lipids and Carbohydrate Metabolism [PDF]

open access: yes, 1957
The purpose of the present study is to reveal the precise mechanism of nervous and humoral regulations of lipid and carbohydrate metabolisms in the adipose tissues.
Awai, Michiyasu   +3 more
core   +1 more source

Adenosine Triphosphatase Activity of the Vascular System.

open access: yesExperimental Biology and Medicine, 1952
SummaryThe AT Pase activity of the vascular system of the dog has been studied, lit has been shown that the enzyme content of -the different arteries enjoys wide variation. The venous system does not contain the enzyme. ATPase activity of the aorta of the rat was not influenced by age or captivity.
Carr Cj   +2 more
openaire   +3 more sources

Histochemical studies of adenosine triphosphatase activity of liver cells exposed to ribonuclease [PDF]

open access: yes, 1962
It has been revealed that ribonuclease (RNase) can penetrate into living cells and inhibits amino acid incorporation into proteins resulting in the suppression of protein synthesis and growth of living cells.
Hayashi, Kenji, Kimoto, Tetsuo
core   +1 more source

Solving the Structure of eIF2 Bound to eIF2B Using Cryogenic Electron Microscopy [PDF]

open access: yes, 2019
Translation begins when initiation factor-2 (eIF2) delivers methionyl initiator tRNA (Met-tRNAi) to the ribosome. The exchange of GDP bound to eIF2 for GTP is a prerequisite to binding Met-tRNAi and is mediated by a second initiation factor, eIF2B ...
Kenner, Lillian
core  

Home - About - Disclaimer - Privacy