Cargando…

LRET-based intramolecular distance measurements in LeuT(Aa)

Detalles Bibliográficos
Autores principales:	Sohail, Azmat, Stolt-Bergner, Peggy, Ecker, Gerhard F, Freissmuth, Michael, Stockner, Thomas, Sitte, Harald H, Sandtner, Walter
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	BioMed Central 2011
Materias:	Meeting Abstract
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3194254/ http://dx.doi.org/10.1186/1471-2210-11-S2-A21

Ejemplares similares

Decrypting structural and functional changes in LeuT(Aa) at atomic level employing LRET
por: Sohail, Azmat, et al.
Publicado: (2012)

Luminescence resonance energy transfer-based intramolecular distance measurements in leucine transporter from Aquifex aeolicus
por: Sohail, Azmat, et al.
Publicado: (2010)

LRET-based distance measurements in the mammalian glutamate transporter EAAT3
por: Saha, Kusumika, et al.
Publicado: (2012)

The Environment Shapes the Inner Vestibule of LeuT
por: Sohail, Azmat, et al.
Publicado: (2016)

The Amino Terminus of LeuT Changes Conformation in an Environment Sensitive Manner
por: Khan, Jawad A., et al.
Publicado: (2019)

Deciphering structural rearrangements during transport process in the bacterial transporter GltPh, homolog to mammalian glutamate transporter
por: Venkatesan, SanthoshKannan, et al.
Publicado: (2012)

Identifying forces that stabilize the oligomeric state of bacterial homologs of neurotransmitter transporters
por: Jayaraman, Kumaresan, et al.
Publicado: (2012)

Refinement of the Central Steps of Substrate Transport by the Aspartate Transporter GltPh: Elucidating the Role of the Na2 Sodium Binding Site
por: Venkatesan, SanthoshKannan, et al.
Publicado: (2015)

To be, or not to be two sites: that is the question about LeuT substrate binding
por: Reyes, Nicolas, et al.
Publicado: (2011)

Conformational dynamics of ligand-dependent alternating access in LeuT
por: Kazmier, Kelli, et al.
Publicado: (2014)

Mutations in the amino-terminus impair amphetamine-induced efflux by inducing inward-facing conformations of the serotonin transporter
por: Sucic, Sonja, et al.
Publicado: (2009)

Substrate-modulated unwinding of transmembrane helices in the NSS transporter LeuT
por: Merkle, Patrick S., et al.
Publicado: (2018)

Experimental conditions can obscure the second high-affinity site in LeuT
por: Quick, Matthias, et al.
Publicado: (2012)

Role of Annular Lipids in the Functional Properties of Leucine Transporter LeuT Proteomicelles
por: LeVine, Michael V., et al.
Publicado: (2016)

Crystal structures of LeuT reveal conformational dynamics in the outward-facing states
por: Fan, Jianjun, et al.
Publicado: (2021)

A comparative study of structures and structural transitions of secondary transporters with the LeuT fold
por: Jeschke, Gunnar
Publicado: (2012)

Resculpting the binding pocket of APC superfamily LeuT-fold amino acid transporters
por: Edwards, Noel, et al.
Publicado: (2017)

Shared dynamics of LeuT superfamily members and allosteric differentiation by structural irregularities and multimerization
por: Ponzoni, Luca, et al.
Publicado: (2018)

The Membrane Protein LeuT in Micellar Systems: Aggregation Dynamics and Detergent Binding to the S2 Site
por: Khelashvili, George, et al.
Publicado: (2013)

Direct assessment of substrate binding to the Neurotransmitter:Sodium Symporter LeuT by solid state NMR
por: Erlendsson, Simon, et al.
Publicado: (2017)

Mutations in the Carboxyl-terminal SEC24 Binding Motif of the Serotonin Transporter Impair Folding of the Transporter
por: El-Kasaby, Ali, et al.
Publicado: (2010)

The high-affinity binding site for tricyclic antidepressants resides in the outer vestibule of the serotonin transporter
por: Sarker, Subhodeep, et al.
Publicado: (2010)

Neurotransmitter/sodium symporter orthologue LeuT has a single high–affinity substrate site
por: Piscitelli, Chayne L., et al.
Publicado: (2010)

Simulated annealing reveals the kinetic activity of SGLT1, a member of the LeuT structural family
por: Longpré, Jean-Philippe, et al.
Publicado: (2012)

A conserved leucine occupies the empty substrate site of LeuT in the Na(+)-free return state
por: Malinauskaite, Lina, et al.
Publicado: (2016)

X-ray structure of LeuT in an inward-facing occluded conformation reveals mechanism of substrate release
por: Gotfryd, Kamil, et al.
Publicado: (2020)

A relationship between membrane permeability of amphetamines and serotonin efflux via serotonin transporters
por: Sandtner, Walter, et al.
Publicado: (2009)

Complete Mapping of Substrate Translocation Highlights the Role of LeuT N-terminal Segment in Regulating Transport Cycle
por: Cheng, Mary Hongying, et al.
Publicado: (2014)

A partially-open inward-facing intermediate conformation of LeuT is associated with Na(+) release and substrate transport
por: Terry, Daniel S., et al.
Publicado: (2018)

Conformation of membrane-inserted P-glycoprotein
por: Stockner, Thomas, et al.
Publicado: (2010)

Mutational Analysis of the High-Affinity Zinc Binding Site Validates a Refined Human Dopamine Transporter Homology Model
por: Stockner, Thomas, et al.
Publicado: (2013)

Microseconds Simulations Reveal a New Sodium-binding Site and the Mechanism of Sodium-coupled Substrate Uptake by LeuT
por: Zomot, Elia, et al.
Publicado: (2015)

Locking Two Rigid-body Bundles in an Outward-Facing Conformation: The Ion-coupling Mechanism in a LeuT-fold Transporter
por: Li, Jing, et al.
Publicado: (2019)

Unifying Concept of Serotonin Transporter-associated Currents
por: Schicker, Klaus, et al.
Publicado: (2012)

Tabulature de leut
por: Ripa, Alberto da, d. 1551
Publicado: (1990)

The N-terminus acts as a lever to support amphetamine-induced substrate efflux by the serotonin transporter
por: Sucic, Sonja, et al.
Publicado: (2012)

NbIT - A New Information Theory-Based Analysis of Allosteric Mechanisms Reveals Residues that Underlie Function in the Leucine Transporter LeuT
por: LeVine, Michael V., et al.
Publicado: (2014)

Differential regulation of amphetamine-induced serotonergic and dopaminergic efflux by syntaxin 1A
por: Montgomery, Therese, et al.
Publicado: (2011)

Calmodulin kinase II regulates amphetamine-induced reverse transport in the dopamine transporter: implications for the importance of the dopamine transporter in Angelman syndrome
por: Steinkellner, Thomas, et al.
Publicado: (2010)

Active transport of rhodamine 123 by the human multidrug transporter P‐glycoprotein involves two independent outer gates
por: Nasim, Fauzia, et al.
Publicado: (2020)

Cannot write session to /tmp/vufind_sessions/sess_39k94ijgff1pdhravnl76ejqb5