Results 31 to 40 of about 3,681,813 (263)
Bioscience Reports, 1988 The importance of protein folding in the biosynthesis of proteins is reviewed.
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An isoform of 14‐3‐3 protein regulates transbilayer lipid movement at the plasma membrane
FEBS Letters, EarlyView.Loss of 14‐3‐3ζ in CHO cells confers resistance to exogenous phosphatidylserine (PS) and impairs endocytosis‐independent inward flip‐flop of fluorescent PS at the plasma membrane. RNAi‐mediated knockdown reproduces this defect, while no additive effect is seen in ATP11C‐deficient cells.
Akiko Yamaji‐Hasegawa +3 more
wiley +1 more source
Intramolecular quality control: HIV-1 envelope gp160 signal-peptide cleavage as a functional folding checkpoint [PDF]
, 2021 Removal of the membrane-tethering signal peptides that target secretory proteins to the endoplasmic reticulum is a prerequisite for proper folding.
Sub Cellular Protein Chemistry +10 more
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FEBS Letters, EarlyView.Plasma membranes contain dynamic nanoscale domains that organize lipids and receptors. Because viruses operate at similar scales, this architecture shapes early infection steps, including attachment, receptor engagement, and entry. Using influenza A virus and HIV‐1 as examples, we highlight how receptor nanoclusters, multivalent glycan interactions ...
Jan Schlegel, Christian Sieben
wiley +1 more source
On the entropy of protein folding [PDF]
Protein Science, 1996 AbstractThe failure to appreciate that the hydration of polar groups is a major contribution to the entropy of protein unfolding has led to considerable underestimates for the loss of configurational freedom when a protein chain folds.
G I, Makhatadze, P L, Privalov
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FEBS Letters, EarlyView.This study reveals that the small GTPase Rab14 is necessary for human papillomavirus (HPV) infection and plays an essential role in the transport of virions to the trans‐Golgi network (TGN). HPV in the early endosome (EE), which harbors GTP‐bound Rab14, is transported to the TGN through the switch of Rab14 from its GTP‐bound to GDP‐bound form.
Yoshiyuki Ishii, Iwao Kukimoto
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Relative domain folding and stability of a membrane transport protein [PDF]
, 2014 There is a limited understanding of the folding of multidomain membrane proteins. Lactose permease (LacY) of Escherichia coli is an archetypal member of the major facilitator superfamily of membrane transport proteins, which contain two domains of six ...
Findlay, Heather E. +8 more
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Degradation mechanism of the von Willebrand factor A2 domain by nattokinase
FEBS Letters, EarlyView.Nattokinase, a natto‐derived protease, exhibits potent antithrombotic effects. This study demonstrates that nattokinase directly cleaves the von Willebrand factor (vWF) A2 domain in vitro. Unlike the native regulator ADAMTS13, nattokinase degrades folded vWF independently of shear stress.
Ryuichi Hyakumoto +3 more
wiley +1 more source
Exploring Protein Sequence Space Using Computationally Directed Recombination [PDF]
, 2006 Evolution has provided us with many protein sequences. However, these sequences represent a very small fraction of the possible sequences. In the laboratory, scientists have explored areas of sequence space not represented by natural proteins both to ...
Meyer, Michelle Margaret
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Annual Review of BiophysicsGlobular proteins are expected to assume folds with fixed secondary structures, α-helices and β-sheets. Fold-switching proteins challenge this expectation by remodeling their secondary and/or tertiary structures in response to cellular stimuli. Though these shape-shifting proteins were once thought to be haphazard evolutionary by-products with little ...
Chakravarty, Devlina, Porter, Lauren L.
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