Results 81 to 90 of about 156,998 (303)

Preclinical Evaluation of Ureidosulfamate Carbonic Anhydrase IX/XII Inhibitors in the Treatment of Cancers [PDF]

open access: yes, 2019
Carbonic anhydrases (CAs) are a family of enzymes involved in the pH regulation of metabolically active cells/tissues. Upregulation of the CAIX/XII isoforms is associated with hypoxic tumours and clinically linked with malignant progression, treatment ...
Gieling, Roben, Williams, Kaye J.
core   +2 more sources

Hippo pathway at the crossroads of stemness and therapeutic resistance in breast cancer

open access: yesMolecular Oncology, EarlyView.
Dysregulation of the Hippo pathway drives nuclear accumulation of YAP/TAZ, activating stemness‐related transcriptional programs that sustain breast cancer stemness and fuel therapeutic resistance across subtypes, underscoring Hippo signaling as a targetable vulnerability. Figure created and edited with BioRender.com.
Giulia Schiavoni   +11 more
wiley   +1 more source

Yeast TLDc domain proteins regulate assembly state and subcellular localization of the V-ATPase

open access: yesThe EMBO Journal
Yeast vacuoles perform crucial cellular functions as acidic degradative organelles, storage compartments, and signaling hubs. These functions are mediated by important protein complexes, including the vacuolar-type H+-ATPase (V-ATPase), responsible for ...
Samira Klössel   +6 more
doaj   +1 more source

The vacuolar-ATPase complex and assembly factors, TMEM199 and CCDC115, control HIF1α prolyl hydroxylation by regulating cellular iron levels

open access: yeseLife, 2017
Hypoxia Inducible transcription Factors (HIFs) are principally regulated by the 2-oxoglutarate and Iron(II) prolyl hydroxylase (PHD) enzymes, which hydroxylate the HIFα subunit, facilitating its proteasome-mediated degradation.
Anna L Miles   +3 more
doaj   +1 more source

Regulation of V-ATPase Activity and Organelle pH by Phosphatidylinositol Phosphate Lipids

open access: yesFrontiers in Cell and Developmental Biology, 2020
Luminal pH and the distinctive distribution of phosphatidylinositol phosphate (PIP) lipids are central identifying features of organelles in all eukaryotic cells that are also critical for organelle function.
Subhrajit Banerjee, Patricia M. Kane
doaj   +1 more source

Molecular basis for the binding and modulation of V-ATPase by a bacterial effector protein. [PDF]

open access: yesPLoS Pathogens, 2017
Intracellular pathogenic bacteria evade the immune response by replicating within host cells. Legionella pneumophila, the causative agent of Legionnaires' Disease, makes use of numerous effector proteins to construct a niche supportive of its replication
Jianhua Zhao   +11 more
doaj   +1 more source

V-ATPase-Mediated Granular Acidification Is Regulated by the V-ATPase Accessory Subunit Ac45 in POMC-Producing Cells [PDF]

open access: yesMolecular Biology of the Cell, 2010
The vacuolar (H+)-ATPase (V-ATPase) is an important proton pump, and multiple critical cell-biological processes depend on the proton gradient provided by the pump. Yet, the mechanism underlying the control of the V-ATPase is still elusive but has been hypothesized to involve an accessory subunit of the pump.
Jansen, E.J.S.   +3 more
openaire   +4 more sources

Transcriptional profiling of circulating extracellular vesicles from prebiopsy prostate cancer patients

open access: yesMolecular Oncology, EarlyView.
RNA profiling of circulating extracellular vesicles (EVs) from blood samples of men undergoing prostate biopsy identifies transcripts associated with clinically significant prostate cancer. Integrative analysis with public tumor datasets links EV‐derived gene signatures to tumor stage and progression‐free survival, highlighting CASP3, XRCC2, and RIT1 ...
Stefan Werner   +14 more
wiley   +1 more source

コウボ エキホウマク ATPase ノ コウゾウ ト キノウ [PDF]

open access: yes, 2005
The yeast vacuolar membrane H+-ATPase (V-ATPase) is the first member of "vacuolar type" ATPase family that has been successively identified in various endocytic and exocytic membrane compartments of eukaryotic cells.
Yasuhiro Anraku   +2 more
core  

Calcium release through P2X4 activates calmodulin to promote endolysosomal membrane fusion [PDF]

open access: yes, 2015
Intra-endolysosomal Ca(2+) release is required for endolysosomal membrane fusion with intracellular organelles. However, the molecular mechanisms for intra-endolysosomal Ca(2+) release and the downstream Ca(2+) targets involved in the fusion remain ...
Baars   +70 more
core   +1 more source

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