Results 31 to 40 of about 156,745 (364)

Human ATP-binding cassette (ABC) transporter family [PDF]

open access: yesHuman Genomics, 2008
There exist four fundamentally different classes of membrane-bound transport proteins: ion channels; transporters; aquaporins; and ATP-powered pumps. ATP-binding cassette (ABC) transporters are an example of ATP-dependent pumps. ABC transporters are ubiquitous membrane-bound proteins, present in all prokaryotes, as well as plants, fungi, yeast and ...
Vasilis Vasiliou   +2 more
openaire   +4 more sources

Structural basis for the mechanism of ABC transporters. [PDF]

open access: yes, 2015
The ATP-binding cassette (ABC) transporters are primary transporters that couple the energy stored in adenosine triphosphate (ATP) to the movement of molecules across the membrane.
Beis, K
core   +1 more source

Cardiac PET Imaging of ATP Binding Cassette (ABC) Transporters: Opportunities and Challenges

open access: yesPharmaceuticals, 2023
Adenosine triphosphate binding cassette (ABC) transporters are a broad family of membrane protein complexes that use energy to transport molecules across cells and/or intracellular organelle lipid membranes. Many drugs used to treat cardiac diseases have
Wanling Liu   +4 more
doaj   +1 more source

Unidirectional Transport Mechanism in an ATP Dependent Exporter [PDF]

open access: yes, 2017
ATP-binding cassette (ABC) transporters use the energy of ATP binding and hydrolysis to move a large variety of compounds across biological membranes.
Bernèche, Simon   +2 more
core   +4 more sources

A single power stroke by ATP binding drives substrate translocation in a heterodimeric ABC transporter

open access: yeseLife, 2020
ATP-binding cassette (ABC) transporters constitute the largest family of primary active transporters, responsible for many physiological processes and human maladies.
Erich Stefan   +2 more
doaj   +1 more source

Boosted coupling of ATP hydrolysis to substrate transport upon cooperative estradiol-17-beta-D-glucuronide binding in a Drosophila ATP binding cassette type-C transporter [PDF]

open access: yes, 2018
ATP binding cassette type-C (ABCC) transporters move molecules across cell membranes upon hydrolysis of ATP; however, their coupling of ATP hydrolysis to substrate transport remains elusive.
Arányi, Tamás   +5 more
core   +1 more source

H-loop Histidine Catalyzes ATP Hydrolysis in the E. coli ABC-Transporter HlyB [PDF]

open access: yesPhys. Chem. Chem. Phys. 2013, 15, 15811-15815, 2013
Adenosine triphosphate (ATP)-binding cassette (ABC) transporters form a family of molecular motor proteins that couple ATP hydrolysis to substrate translocation across cell membranes. Each nucleotide binding domain of ABC-transporters contains a highly conserved H-loop Histidine residue, whose precise mechanistic role to motor functions has remained ...
arxiv   +1 more source

ATP-binding cassette transporters in Escherichia coli

open access: yesBiochimica et Biophysica Acta (BBA) - Biomembranes, 2008
ATP-binding cassette (ABC) transporters are integral membrane proteins that actively transport molecules across cell membranes. In Escherichia coli they consist primarily of import systems that involve in addition to the ABC transporter itself a substrate binding protein and outer membrane receptors or porins, and a number of transporters with varied ...
Moussatova, Anastassiia   +3 more
openaire   +4 more sources

Jadomycins: A potential chemotherapy for multi‐drug resistant metastatic breast cancer

open access: yesPharmacology Research & Perspectives, 2021
Breast cancer causes the most cancer fatalities in women worldwide. Approximately one‐third of breast cancers metastasize, or spread from primary tumors to other tissues, and have a 70% 5‐year mortality rate.
Esther P. Bonitto   +2 more
doaj   +1 more source

Structures and functions of mitochondrial ABC transporters [PDF]

open access: yes, 2015
A small number of physiologically important ATP-binding cassette (ABC) transporters are found in mitochondria. Most are half transporters of the B group forming homodimers and their topology suggests they function as exporters.
Aller   +67 more
core   +2 more sources

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