Archazolid A binds to the equatorial region of the c-ring of the vacuolar H+-ATPase. - Wikidata - awgldk - TriplyDB

Archazolid A binds to the equatorial region of the c-ring of the vacuolar H+-ATPase.

Archazolid A binds to the equatorial region of the c-ring of the vacuolar H+-ATPase.

http://www.wikidata.org/entity/Q41500748

about

PA1b inhibitor binding to subunits c and e of the vacuolar ATPase reveals its insecticidal mechanism Inhibitors of V-ATPase proton transport reveal uncoupling functions of tether linking cytosolic and membrane domains of V0 subunit a (Vph1p).Mutations in the proteolipid subunits of the vacuolar H+-ATPase provide resistance to indolotryptoline natural products.Synthesis of the C1-C17 fragment of the archazolids by complex cis-homodimer cross metathesis.V-ATPase inhibition increases cancer cell stiffness and blocks membrane related Ras signaling - a new option for HCC therapy.Recent Insights into the Structure, Regulation, and Function of the V-ATPases Total syntheses of the archazolids: an emerging class of novel anticancer drugs.Anti-leukemic effects of the V-ATPase inhibitor Archazolid A.Resistance mechanisms of cancer cells to the novel vacuolar H(+)-ATPase inhibitor archazolid B.Natural products from myxobacteria: novel metabolites and bioactivities.V-ATPase inhibition by archazolid leads to lysosomal dysfunction resulting in impaired cathepsin B activation in vivo.Mode of cell death induction by pharmacological vacuolar H+-ATPase (V-ATPase) inhibition.Synthesis and activity of the archazolid western hemisphere.MDM2 antagonist nutlin-3a sensitizes tumors to V-ATPase inhibition.EPR Studies of V-ATPase with Spin-Labeled Inhibitors DCC and Archazolid: Interaction Dynamics with Proton Translocating Subunit c.The binding site of the V-ATPase inhibitor apicularen is in the vicinity of those for bafilomycin and archazolid.Reversible disassembly of the yeast V-ATPase revisited under in vivo conditions.Hyperacidification of trans-Golgi network and endo/lysosomes in melanocytes by glucosylceramide-dependent V-ATPase activity.The vacuolar-type ATPase inhibitor archazolid increases tumor cell adhesion to endothelial cells by accumulating extracellular collagen Vacuolar H+-ATPase: An Essential Multitasking Enzyme in Physiology and Pathophysiology

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P2860

Archazolid A binds to the equatorial region of the c-ring of the vacuolar H+-ATPase.

http://www.wikidata.org/entity/Q41500748

description

2010 nî lūn-bûn

@nan

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

2010年论文

@zh

2010年论文

@zh-cn

name

Archazolid A binds to the equatorial region of the c-ring of the vacuolar H+-ATPase.

@en

Archazolid A binds to the equatorial region of the c-ring of the vacuolar H+-ATPase.

@en-gb

type

label

Archazolid A binds to the equatorial region of the c-ring of the vacuolar H+-ATPase.

@en

Archazolid A binds to the equatorial region of the c-ring of the vacuolar H+-ATPase.

@en-gb

prefLabel

Archazolid A binds to the equatorial region of the c-ring of the vacuolar H+-ATPase.

@en

Archazolid A binds to the equatorial region of the c-ring of the vacuolar H+-ATPase.

@en-gb

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P356

JBC.M110.137539

P1433

Journal of Biological Chemistry

P1476

Archazolid A binds to the equatorial region of the c-ring of the vacuolar H+-ATPase.

@en

P2093

Dirk Menche

http://www.w3.org/2001/XMLSchema#string

Helmut Wieczorek

http://www.w3.org/2001/XMLSchema#string

Markus Huss

http://www.w3.org/2001/XMLSchema#string

Paultheo von Zezschwitz

http://www.w3.org/2001/XMLSchema#string

Sven Rudolph

http://www.w3.org/2001/XMLSchema#string

Svenja Bockelmann

http://www.w3.org/2001/XMLSchema#string

Tobias Bender

http://www.w3.org/2001/XMLSchema#string

P2860

Archazolid and apicularen: novel specific V-ATPase inhibitors

Protein structure prediction on the Web: a case study using the Phyre server

Purification and properties of H+-translocating, Mg2+-adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae.

The vacuolar (H+)-ATPases--nature's most versatile proton pumps

Cryo-electron microscopy of the vacuolar ATPase motor reveals its mechanical and regulatory complexity

Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo

Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology

Concanamycin A, the specific inhibitor of V-ATPases, binds to the V(o) subunit c.

Disruption of genes encoding subunits of yeast vacuolar H(+)-ATPase causes conditional lethality.

Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae.

P304

38304-38314

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scholarly article

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10.1074/JBC.M110.137539

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P433

49

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P478

285

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P50

Stephanie Grond

P577

2010-09-30T00:00:00Z

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P698

20884613

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2992264

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