Journal ArticleDOI
Coiled coils - new structures and new functions
TLDR
The structures of more than 20 proteins containing coiled-coil domains have been solved to high resolution and provided many new insights into the structure of coiled coils, their discontinuities, their relationship with other helical bundles and the problems connected with their prediction from protein sequences.About:
This article is published in Trends in Biochemical Sciences.The article was published on 1996-10-01. It has received 1279 citations till now. The article focuses on the topics: Knobs into holes packing & Coiled coil.read more
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The WRKY superfamily of plant transcription factors
TL;DR: The WRKY proteins are a superfamily of transcription factors with up to 100 representatives in Arabidopsis that appear to be involved in the regulation of various physio-logical programs that are unique to plants, including pathogen defense, senescence and trichome development.
Journal ArticleDOI
Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
TL;DR: It is concluded that Mfn1 and Mfn2 have both redundant and distinct functions and act in three separate molecular complexes to promote mitochondrial fusion, and by enabling cooperation between mitochondria, has protective effects on the mitochondrial population.
Journal ArticleDOI
Rho GTPases and their effector proteins.
Anne L. Bishop,Alan Hall +1 more
TL;DR: The main focus of this review will be Rho, Rac and Cdc42, the three best characterized mammalian Rho GTPases, though the genetic analysis of RhoGTPases in lower eukaryotes is making increasingly important contributions to this field.
Journal ArticleDOI
MEMBRANE PROTEIN FOLDING AND STABILITY: Physical Principles
TL;DR: A coherent thermodynamic formalism for determining and describing the energetics of peptide-bilayer interactions and a review of the properties of the environment of membrane proteins--the bilayer milieu are reviewed.
Journal ArticleDOI
The tripartite motif family identifies cell compartments.
Alexandre Reymond,Germana Meroni,Anna Fantozzi,Giuseppe Merla,Stefano Cairo,Lucilla Luzi,Daniela Riganelli,Elena Zanaria,Silvia Messali,Silvia Cainarca,Alessandro Guffanti,Saverio Minucci,Pier Giuseppe Pelicci,Andrea Ballabio +13 more
TL;DR: The results demonstrate that TRIM proteins share a common function: by means of homo‐multimerization they identify specific cell compartments.
References
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The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins
TL;DR: A 30-amino-acid segment of C/EBP, a newly discovered enhancer binding protein, shares notable sequence similarity with a segment of the cellular Myc transforming protein, and may represent a characteristic property of a new category of DNA binding proteins.
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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.
TL;DR: The crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 Å resolution supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant.
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Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution.
TL;DR: The haemagglutinin glycoprotein of influenza virus is a trimer comprising two structurally distinct regions: a triple-stranded coiled-coil of α-helices extends 76 Å from the membrane and a globular region of antiparallel β-sheet is positioned on top of this stem.
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Structure of influenza haemagglutinin at the pH of membrane fusion
TL;DR: Low pH induces a conformational change in the influenza virus haemagglutinin, which then mediates fusion of the viral and host cell membranes, and reveals a major refolding of the secondary and tertiary structure of the molecule.
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A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
TL;DR: These studies demonstrate that conserved, buried residues in the GCN4 leucine zipper direct dimer formation are essential determinants of the global fold.