Results 111 to 120 of about 5,149,379 (301)

Smaller is better: nanobodies meet NMR

open access: yesFEBS Letters, EarlyView.
Nanobodies are single‐domain antigen‐binding fragments derived from camelid heavy chain antibodies. Their small size, high stability, and exceptional specificity make nanobodies uniquely useful probes for NMR studies of protein dynamics, transient conformational states, and protein–protein interactions.
Oleg Y. Dmitriev
wiley   +1 more source

Biochemical and functional studies of a novel complement inhibitor, CRIT, with its interaction partners [PDF]

open access: yes, 2005
Complement C2 receptor trispanning (CRIT), a three transmembrane receptor, was first discovered on the surface of the parasite Schistosoma haematobium and formerly termed Schistosoma trispanning orphan receptor (Sh-TOR). This receptor acts as decoy C2-
Hui, Kwok-Min
core   +1 more source

Two Receptor Binding Strategy of SARS-CoV-2 Is Mediated by Both the N-Terminal and Receptor-Binding Spike Domain [PDF]

open access: yesThe Journal of Physical Chemistry B
It is not well understood why severe acute respiratory syndrome (SARS)-CoV-2 spreads much faster than other β-coronaviruses such as SARS-CoV and Middle East respiratory syndrome (MERS)-CoV. In a previous publication, we predicted the binding of the N-terminal domain (NTD) of SARS-CoV-2 spike to sialic acids (SAs).
Michele Monti   +18 more
openaire   +3 more sources

Neutralization of the PTX3/CD44 axis suppresses TGF‐β1 signaling in kidney fibrosis

open access: yesFEBS Letters, EarlyView.
This study investigates how the PTX3/CD44 axis promotes kidney fibrosis by activating TGF‐β1 signaling. We demonstrate that the neutralizing antibody WHC‐001 effectively inhibits this pathway, suppressing myofibroblast activation and partial epithelial–mesenchymal transition (EMT).
Chao‐Chun Cheng   +8 more
wiley   +1 more source

Role of CD4 epitopes outside the gp120-binding site during entry of human immunodeficiency virus type 1 [PDF]

open access: yes, 1997
CD4 is the primary receptor for human immunodeficiency virus (HIV). The binding site for the surface glycoprotein of HIV type 1 (HIV-1), gp120, has been mapped to the C'-C" region of domain 1 of CD4. Previously, we have shown that a mutant of rat CD4, in
Puklavec, M.   +7 more
core  

Complex formation of EphB1/Nck/Caskin1 leads to tyrosine phosphorylation and structural changes of the Caskin1 SH3 domain. [PDF]

open access: yes, 2012
Scaffold proteins have an important role in the regulation of signal propagation. These proteins do not possess any enzymatic activity but can contribute to the formation of multiprotein complexes.
Roopesh Udupa   +16 more
core   +1 more source

Going viral − Virus‐targeting nanobodies for research, diagnostics and therapy

open access: yesFEBS Letters, EarlyView.
The increasing prevalence of viral diseases represents a major threat for global human health. Nanobodies, small binding fragments derived from camelid heavy‐chain antibodies, offer versatile tools for viral research, diagnostics, and antiviral therapy.
Domenic Ebert, Ulrich Rothbauer
wiley   +1 more source

Structural and functional analysis of the heparin-binding domain of VEGF164. [PDF]

open access: yes, 2006
Several of the multitude of functions attributed to Vascular Endothelial Growth Factor-A (VEGF-A) are coordinated by its various isoforms, which are generated as a result of alternative splicing from a single gene. Despite the fact that the VEGF isoforms
Krilleke, D.
core  

The role of ECL2 in CGRP receptor activation: a combined modelling and experimental approach [PDF]

open access: yes, 2013
The calcitonin gene-related peptide (CGRP) receptor is a complex of a calcitonin receptor-like receptor (CLR), which is a family B G-protein-coupled receptor (GPCR) and receptor activity modifying protein 1.
Poyner, David   +18 more
core   +1 more source

Soft motions encoded by the fold and mediated by conserved hinge sites drive V‐ATPase allosteric machinery and autoinhibition

open access: yesFEBS Letters, EarlyView.
Vacuolar H+‐ATPase (V‐ATPase) is a multisubunit rotary proton pump that acidifies intracellular compartments. Using elastic network models, we identified conserved hinge residues that govern its large‐scale functional motions. We show that intrinsically encoded ‘soft modes’ drive critical functional transitions, including rotary catalysis and ...
Diksha Parwana   +3 more
wiley   +1 more source

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