Coloured computergraphic displays of subunit-subunit interfaces of oligomeric proteins

1984 ◽  
Vol 12 (2) ◽  
pp. 285-285 ◽  
Author(s):  
E. JAMES MILNER-WHITE
Keyword(s):  
Oligomeric Proteins

scholarly journals Equilibria of oligomeric proteins under high pressure – A theoretical description

2016 ◽  
Vol 411 ◽  
pp. 16-26 ◽  
Author(s):  
Marek Ingr ◽  
Eva Kutálková ◽  
Josef Hrnčiřík ◽  
Reinhard Lange
Keyword(s):  
High Pressure ◽  
Theoretical Description ◽  
Oligomeric Proteins

scholarly journals Breaking in and busting out: cell-penetrating peptides and the endosomal escape problem

2017 ◽  
Vol 8 (3-4) ◽  
pp. 131-141 ◽  
Author(s):  
Julia C. LeCher ◽  
Scott J. Nowak ◽  
Jonathan L. McMurry
Keyword(s):  
Cell Penetrating Peptides ◽  
Endosomal Escape ◽  
Great Promise ◽  
Delivery Methods ◽  
Oligomeric Proteins ◽  
Cell Penetrating ◽  
History Of ◽  
A Cell ◽  
Escape Problem ◽  
Primary Focus

AbstractCell-penetrating peptides (CPPs) have long held great promise for the manipulation of living cells for therapeutic and research purposes. They allow a wide array of biomolecules from large, oligomeric proteins to nucleic acids and small molecules to rapidly and efficiently traverse cytoplasmic membranes. With few exceptions, if a molecule can be associated with a CPP, it can be delivered into a cell. However, a growing realization in the field is that CPP-cargo fusions largely remain trapped in endosomes and are eventually targeted for degradation or recycling rather than released into the cytoplasm or trafficked to a desired subcellular destination. This ‘endosomal escape problem’ has confounded efforts to develop CPP-based delivery methods for drugs, enzymes, plasmids, etc. This review provides a brief history of CPP research and discusses current issues in the field with a primary focus on the endosomal escape problem, for which several promising potential solutions have been developed. Are we on the verge of developing technologies to deliver therapeutics such as siRNA, CRISPR/Cas complexes and others that are currently failing because of an inability to get into cells, or are we just chasing after another promising but unworkable technology? We make the case for optimism.

Oligomeric Proteins

2013 ◽  
pp. 1781-1789
Author(s):  
Richard C. Garratt ◽  
Napoleão Fonseca Valadares ◽  
José Fernando Ruggiero Bachega
Keyword(s):  
Oligomeric Proteins

scholarly journals A biophysical and structural analysis of DNA binding by oligomeric hSSB1 (NABP2/OBFC2B)

2020 ◽  
Author(s):  
Serene El-Kamand ◽  
Slobodan Jergic ◽  
Teegan Lawson ◽  
Ruvini Kariawasam ◽  
Derek J. Richard ◽  
...  
Keyword(s):  
Dna Binding ◽  
Oxidative Dna Damage ◽  
Genomic Stability ◽  
Dna Binding Protein ◽  
Oxidative Modification ◽  
Dna Bases ◽  
Genome Integrity ◽  
Oligomeric Proteins ◽  
Ssdna Binding ◽  
Dna Strands

AbstractThe oxidative modification of DNA can result in the loss of genome integrity and must be repaired to maintain overall genomic stability. We have recently demonstrated that human single stranded DNA binding protein 1 (hSSB1/NABP2/OBFC2B) plays a crucial role in the removal of 8-oxo-7,8-dihydro- guanine (8-oxoG), the most common form of oxidative DNA damage. The ability of hSSB1 to form disulphide-bonded tetramers and higher oligomers in an oxidative environment is critical for this process. In this study, we have used nuclear magnetic resonance (NMR) spectroscopy and surface plasmon resonance (SPR) experiments to determine the molecular details of ssDNA binding by oligomeric hSSB1. We reveal that hSSB1 oligomers interact with single DNA strands containing damaged DNA bases; however, our data also show that oxidised bases are recognised in the same manner as undamaged DNA bases. We further demonstrate that oxidised hSSB1 interacts with ssDNA with a significantly higher affinity than its monomeric form confirming that oligomeric proteins such as tetramers can bind directly to ssDNA. NMR experiments provide evidence that oligomeric hSSB1 is able to bind longer ssDNA in both binding polarities using a distinct set of residues different to those of the related SSB from Escherichia coli.

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