Results 81 to 90 of about 174,472 (299)
Molecular Oncology, EarlyView.Methods to improve antibody–drug conjugate (ADC) treatment durability in cancer therapy are needed. We utilized ADCs and immune‐stimulating antibody conjugates (ISACs), which are made from two non‐competitive antibodies, to enhance the entry of toxic payloads into cancer cells and deliver immunostimulatory agents into immune cells.
Tiexin Wang +3 more
wiley +1 more source
3.5Å cryoEM structure of hepatitis B virus core assembled from full-length core protein. [PDF]
, 2013 The capsid shell of infectious hepatitis B virus (HBV) is composed of 240 copies of a single protein called HBV core antigen (HBc). An atomic model of a core assembled from truncated HBc was determined previously by X-ray crystallography.
Jih, Jonathan +4 more
core
Functional divergence in the role of N-linked glycosylation in smoothened signaling [PDF]
, 2015 The G protein-coupled receptor (GPCR) Smoothened (Smo) is the requisite signal transducer of the evolutionarily conserved Hedgehog (Hh) pathway. Although aspects of Smo signaling are conserved from Drosophila to vertebrates, significant differences have ...
A Helenius +83 more
core +3 more sources
Disulfide Bonds in Sendai Virus Glycoproteins
Intervirology, 1979 The precursor of fusion protein (Fo) in Sendai virus growth in Vero cells can be cleaved by trypsin to forms F1 and F2, which can be resolved on SDS-polyacrylamide gels. However, if disulfide bonds are preserved during electrophoresis, F1 and F2 remain linked together even after trypsin treatment (F).
J M, Hardwick, R H, Bussell
openaire +2 more sources
Amino Acid Patterns around Disulfide Bonds [PDF]
International Journal of Molecular Sciences, 2010 Disulfide bonds provide an inexhaustible source of information on molecular evolution and biological specificity. In this work, we described the amino acid composition around disulfide bonds in a set of disulfide-rich proteins using appropriate descriptors, based on ANOVA (for all twenty natural amino acids or classes of amino acids clustered according
José R. F. Marques +3 more
openaire +2 more sources
Raman‐based label‐free microscopic analysis of the pancreas in living zebrafish larvae
FEBS Open Bio, EarlyView.Forward stimulated Raman scattering (F‐SRS) and epi coherent anti‐Stokes Raman scattering (E‐CARS) allow label‐free discrimination of distinct subcellular structures in the pancreas of living zebrafish larvae. Given the straightforward applicability, we anticipate broad implementation of Raman microscopy in other organs and across various biomedical ...
Noura Faraj +3 more
wiley +1 more source
Dithiolopyrrolone Natural Products : Isolation, Synthesis and Biosynthesis [PDF]
, 2013 Peer reviewedPublisher ...
Deng, Hai +3 more
core +2 more sources
FEBS Open Bio, EarlyView.This study explores the feasibility of expressing the antitumoral protein Amblyomin‐X through a suicide gene therapy approach and investigates its intracellular fate after gene delivery. Although the gene is efficiently expressed, melanoma cells rapidly degrade the Amblyomin‐X protein via proteasome activity.
Victor Dal Posolo Cinel +4 more
wiley +1 more source
\u3cem\u3eDrosophila\u3c/em\u3e Vitelline Membrane Assembly: A Critical Role for an Evolutionarily Conserved Cysteine in the “VM domain” of sV23 [PDF]
, 2010 The vitelline membrane (VM), the oocyte proximal layer of the Drosophila eggshell, contains four major proteins (VMPs) that possess a highly conserved “VM domain” which includes three precisely spaced, evolutionarily conserved, cysteines (CX7CX8C ...
Beauchamp, J. M. +3 more
core +1 more source
Bond-selective photodissociation of aliphatic disulfides [PDF]
Journal of the American Society for Mass Spectrometry, 1995 The photochemistry of aliphatic disulfides is presented. The photolysis products are photoionized with coherent vacuum ultraviolet radiation and analyzed by time-of-flight mass spectrometry. With 248-nm excitation, the predominant dissociation pathway is S-S bond cleavage.
Bookwalter, Craig W. +3 more
openaire +2 more sources