Results 31 to 40 of about 5,205,392 (267)

Transient protein-protein interactions [PDF]

open access: yesProtein Engineering Design and Selection, 2011
Transient complexes are crucial for diverse biological processes such as biochemical pathways and signaling cascades in the cell. Here, we give an overview of the transient interactions; the importance of transient interactions as drug targets; and the structural characterization of transient protein-protein complexes based on the geometrical and ...
Saliha Ece, Acuner Ozbabacan   +3 more
openaire   +2 more sources

Structures of the wild-type MexAB–OprM tripartite pump reveal its complex formation and drug efflux mechanism

open access: yesNature Communications, 2019
In Pseudomonas aeruginosa, MexAB–OprM plays a central role in multidrug resistance by ejecting various drug compounds. Here the authors present the structure of wild-type MexAB–OprM in the presence or absence of drugs and propose mechanisms for complex ...
Kenta Tsutsumi   +7 more
doaj   +1 more source

DOCKGROUND Membrane Protein-Protein Set [PDF]

open access: yesPLOS ONE, 2021
ABSTRACTMembrane proteins play essential role in cellular mechanisms. Despite that and the major progress in experimental structure determination, they are still significantly underrepresented in Protein Data Bank. Thus, computational approaches to protein structure determination, which are important in general, are especially valuable in the case of ...
Ian Kotthoff   +2 more
openaire   +4 more sources

The extracellular interactome of the human adenovirus family reveals diverse strategies for immunomodulation

open access: yesNature Communications, 2016
Viruses interact with their hosts via secreted and membrane-bound proteins to affect host immune responses and virulence. Here the authors contribute to our understanding of this relationship with an extracellular interaction map of human and adenoviral ...
Nadia Martinez-Martin   +11 more
doaj   +1 more source

Aquaporin Protein-Protein Interactions [PDF]

open access: yesInternational Journal of Molecular Sciences, 2017
Aquaporins are tetrameric membrane-bound channels that facilitate transport of water and other small solutes across cell membranes. In eukaryotes, they are frequently regulated by gating or trafficking, allowing for the cell to control membrane permeability in a specific manner.
Jennifer Roche   +1 more
openaire   +2 more sources

Time-resolved spectroscopic and electrophysiological data reveal insights in the gating mechanism of anion channelrhodopsin

open access: yesCommunications Biology, 2021
Dreier et al. reports that the anion channelrhodopsin GtACR1 does not undergo a syn-cycle (light adapted ground state) and thus has a more efficient channel behaviour than CrChR2.
Max-Aylmer Dreier   +8 more
doaj   +1 more source

Interfacial Protein–Protein Associations [PDF]

open access: yesBiomacromolecules, 2013
While traditional models of protein adsorption focus primarily on direct protein-surface interactions, recent findings suggest that protein-protein interactions may play a central role. Using high-throughput intermolecular resonance energy transfer (RET) tracking, we directly observed dynamic, protein-protein associations of bovine serum albumin on ...
Blake B, Langdon   +3 more
openaire   +2 more sources

Predicting Antibody Developability Profiles Through Early Stage Discovery Screening

open access: yesmAbs, 2020
Monoclonal antibodies play an increasingly important role for the development of new drugs across multiple therapy areas. The term ‘developability’ encompasses the feasibility of molecules to successfully progress from discovery to development via ...
Marc Bailly   +21 more
doaj   +1 more source

Cryo-EM demonstrates the in vitro proliferation of an ex vivo amyloid fibril morphology by seeding

open access: yesNature Communications, 2022
Here, the authors present the cryo-EM structure of in vitro amyloid fibrils from recombinant SAA1.1 protein that were formed by seeding with fibrils purified from systemic AA amyloidosis tissue.
Thomas Heerde   +12 more
doaj   +1 more source

Structure of cyanobacterial photosystem I complexed with ferredoxin at 1.97 Å resolution

open access: yesCommunications Biology, 2022
In order to aid the understanding of the electron transfer process within the cyanobacterial photosystem I, its structure - when complexed with Ferredoxin - is determined at 1.97 Å resolution.
Jiannan Li   +10 more
doaj   +1 more source

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