Results 11 to 20 of about 723,818 (342)

Protein design is a key factor for subunit–subunit association [PDF]

open access: yesProceedings of the National Academy of Sciences, 1999
Fundamental questions about role of the quaternary structures are addressed by using a statistical mechanics off-lattice model of a dimer protein. The model, in spite of its simplicity, captures key features of the monomer–monomer interactions revealed by atomic force experiments.
C. CLEMENTI, P. CARLONI, MARITAN, AMOS
openaire   +5 more sources

Subunit interactions of the Go protein [PDF]

open access: yesFEBS Letters, 1992
The monoclonal antibody, MONO, recognizes an epitope on the G protein αo‐subunit [van der Voorn et al., submitted] and readily immunoprecipitates heterotrimeric Go proteins from solubilized, crude bovine brain membranes, as well as from a purified bovine brain G protein preparation.
Trudi Hengeveld   +2 more
openaire   +2 more sources

Denervation-induced activation of the standard proteasome and immunoproteasome [PDF]

open access: yes, 2016
The standard 26S proteasome is responsible for the majority of myofibrillar protein degradation leading to muscle atrophy. The immunoproteasome is an inducible form of the proteasome.
Baumann, Cory W.   +3 more
core   +6 more sources

Immunolocalization of KATP channel subunits in mouse and rat cardiac myocytes and the coronary vasculature. [PDF]

open access: yes, 2005
BACKGROUND: Electrophysiological data suggest that cardiac KATP channels consist of Kir6.2 and SUR2A subunits, but the distribution of these (and other KATP channel subunits) is poorly defined.
Artman, M   +13 more
core   +3 more sources

Structural similarity and classification of protein interaction interfaces. [PDF]

open access: yesPLoS ONE, 2011
Interactions between proteins play a key role in many cellular processes. Studying protein-protein interactions that share similar interaction interfaces may shed light on their evolution and could be helpful in elucidating the mechanisms behind ...
Nan Zhao   +3 more
doaj   +1 more source

Subunit Exchange in Protein Complexes

open access: yesJournal of Molecular Biology, 2018
Over the past 50 years, protein complexes have been studied with techniques such as X-ray crystallography and electron microscopy, generating images which although detailed are static and homogeneous. More recently, limited application of in vivo fluorescence and other techniques has revealed that many complexes previously thought stable and ...
Tusk, S, Delalez, N, Berry, R
openaire   +2 more sources

The G Protein γ Subunit [PDF]

open access: yesJournal of Biological Chemistry, 1995
Guanine nucleotide-binding protein beta and gamma subunits form a tightly bound complex that can only be separated by denaturation. Assembly of beta and gamma subunits is a complicated process. The beta 1 and gamma 2 subunits can be synthesized in vitro in rabbit reticulocyte lysate and then assembled into dimers, but beta 1 cannot form beta gamma ...
Denise J. Spring   +4 more
openaire   +3 more sources

The Est3 protein is a subunit of yeast telomerase [PDF]

open access: yesCurrent Biology, 2000
EST1, EST2, EST3 and TLC1 function in a single pathway for telomere replication in the yeast Saccharomyces cerevisiae [1] [2], as would be expected if these genes all encode components of the same complex. Est2p, the reverse transcriptase protein subunit, and TLC1, the templating RNA, are subunits of the catalytic core of yeast telomerase [3] [4] [5 ...
Sara K. Evans   +3 more
openaire   +3 more sources

Characterization of alkali-modified soy protein concentrate [PDF]

open access: yesActa Periodica Technologica, 2005
To study the influence of the preparation mode, including mild alkali modification, of soy protein concentrate on soluble protein content and composition, some of its nutritive and functional properties were investigated. Soy protein concentrate prepared
Barać Miroljub B.   +2 more
doaj   +1 more source

Amino-terminal cysteine residues of RGS16 are required for palmitoylation and modulation of G(i)- and G(q)-mediated signaling [PDF]

open access: yes, 1999
RGS proteins (Regulators of G protein Signaling) are a recently discovered family of proteins that accelerate the GTPase activity of heterotrimeric G protein α subunits of the i, q, and 12 classes.
Backlund, Peter S.   +5 more
core   +1 more source

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