Results 91 to 100 of about 13,339,631 (403)

The likelihood that two proteins interact might depend on the proteins' age [PDF]

open access: yes, 2007
It has been previously shown [1] that _S. cerevisiae_ proteins preferentially interact with proteins of the same estimated likely time of origin. To study this observation further, the protein interaction networks of _S. cerevisiae_ and _H.
Pedro Beltrao
core   +2 more sources

The carboxylate “gripper” of the substrate is critical for C‐4 stereo‐inversion by UDP‐glucuronic acid 4‐epimerase

open access: yesFEBS Letters, EarlyView.
UDP‐glucuronic acid 4‐epimerase (UGAepi) catalyzes NAD+‐dependent interconversion of UDP‐glucuronic acid (UDP‐GlcA) and UDP‐galacturonic acid (UDP‐GalA) via C4‐oxidation, 4‐keto‐intermediate rotation, and C4‐reduction. Here, Borg et al. examined the role of the substrate's carboxylate group in the enzymic mechanism by analyzing NADH‐dependent reduction
Annika J. E. Borg   +2 more
wiley   +1 more source

The unfolding of iRFP713 in a crowded milieu [PDF]

open access: yesPeerJ, 2019
The exploring of biological processes in vitro under conditions of macromolecular crowding is a way to achieve an understanding of how these processes occur in vivo.
Olesya V. Stepanenko   +3 more
doaj   +2 more sources

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   +3 more sources

B cell mechanobiology in health and disease: emerging techniques and insights into therapeutic responses

open access: yesFEBS Letters, EarlyView.
B cells sense external mechanical forces and convert them into biochemical signals through mechanotransduction. Understanding how malignant B cells respond to physical stimuli represents a groundbreaking area of research. This review examines the key mechano‐related molecules and pathways in B lymphocytes, highlights the most relevant techniques to ...
Marta Sampietro   +2 more
wiley   +1 more source

CSF protein biomarkers predicting longitudinal reduction of CSF β-amyloid42 in cognitively healthy elders. [PDF]

open access: yes, 2013
β-amyloid (Aβ) plaque accumulation is a hallmark of Alzheimer's disease (AD). It is believed to start many years prior to symptoms and is reflected by reduced cerebrospinal fluid (CSF) levels of the peptide Aβ1-42 (Aβ42).
Alzheimer's Disease Neuroimaging Initiative   +8 more
core   +1 more source

The thioredoxin‐like and one glutaredoxin domain are required to rescue the iron‐starvation phenotype of HeLa GLRX3 knock out cells

open access: yesFEBS Letters, EarlyView.
Glutaredoxin (Grx) 3 proteins contain a thioredoxin domain and one to three class II Grx domains. These proteins play a crucial role in iron homeostasis in eukaryotic cells. In human Grx3, at least one of the two Grx domains, together with the thioredoxin domain, is essential for its function in iron metabolism.
Laura Magdalena Jordt   +4 more
wiley   +1 more source

Vibrational energy relaxation in proteins

open access: yes, 2005
An overview of theories related to vibrational energy relaxation (VER) in proteins is presented. VER of a selected mode in cytochrome c is studied using two theoretical approaches.
Bu   +24 more
core   +2 more sources

Improved proteomic analysis of nuclear proteins, as exemplified by the comparison of two myelo\"id cell lines nuclear proteomes [PDF]

open access: yes, 2012
One of the challenges of the proteomic analysis by 2D-gel is to visualize the low abundance proteins, particularly those localized in organelles. An additional problem with nuclear proteins lies in their strong interaction with nuclear acids.
Chevallet, Mireille   +5 more
core   +4 more sources

In vivo evidence for glycyl radical insertion into a catalytically inactive variant of pyruvate formate‐lyase

open access: yesFEBS Letters, EarlyView.
Dimeric pyruvate formate‐lyase cleaves pyruvate using a radical‐based mechanism. G734 serves as a radical storage location, and the radical is transferred to the catalytic C419 residue. Mutation of the C418‐C419 pair causes loss of enzyme activity, but does not impede radical introduction onto G734. Therefore, cis‐ but not trans‐radical transfer occurs
Michelle Kammel   +2 more
wiley   +1 more source

Home - About - Disclaimer - Privacy