scholarly journals The Protocol for SNAC-tag Chemical Protein Cleavage

2019 ◽  
Author(s):  
Bobo dang ◽  
Bobo dang ◽  
William DeGrado
Keyword(s):  
Protein Cleavage

scholarly journals Effects of Gag Mutation and Processing on Retroviral Dimeric RNA Maturation

2006 ◽  
Vol 80 (3) ◽  
pp. 1242-1249 ◽  
Author(s):  
William Fu ◽  
Que Dang ◽  
Kunio Nagashima ◽  
Eric O. Freed ◽  
Vinay K. Pathak ◽  
...  
Keyword(s):  
Viral Protein ◽  
Leukemia Virus ◽  
Viral Rna ◽  
Host Cells ◽  
Protein Cleavage ◽  
Rna Packaging ◽  
Virus Rna ◽  
Rna Dimer ◽  
Rna Maturation ◽  
Hiv 1

ABSTRACT After their release from host cells, most retroviral particles undergo a maturation process, which includes viral protein cleavage, core condensation, and increased stability of the viral RNA dimer. Inactivating the viral protease prevents protein cleavage; the resulting virions lack condensed cores and contain fragile RNA dimers. Therefore, protein cleavage is linked to virion morphological change and increased stability of the RNA dimer. However, it is unclear whether protein cleavage is sufficient for mediating virus RNA maturation. We have observed a novel phenotype in a murine leukemia virus capsid mutant, which has normal virion production, viral protein cleavage, and RNA packaging. However, this mutant also has immature virion morphology and contains a fragile RNA dimer, which is reminiscent of protease-deficient mutants. To our knowledge, this mutant provides the first evidence that Gag cleavage alone is not sufficient to promote RNA dimer maturation. To extend our study further, we examined a well-defined human immunodeficiency virus type 1 (HIV-1) Gag mutant that lacks a functional PTAP motif and produces immature virions without major defects in viral protein cleavage. We found that the viral RNA dimer in the PTAP mutant is more fragile and unstable compared with those from wild-type HIV-1. Based on the results of experiments using two different Gag mutants from two distinct retroviruses, we conclude that Gag cleavage is not sufficient for promoting RNA dimer maturation, and we propose that there is a link between the maturation of virion morphology and the viral RNA dimer.

scholarly journals Efficient site specific removal of a C-terminal FLAG fusion from a Fab′ using copper(II) ion catalysed protein cleavage

1999 ◽  
Vol 12 (2) ◽  
pp. 179-184 ◽  
Author(s):  
David P. Humphreys ◽  
Bryan J. Smith ◽  
Lloyd M. King ◽  
Shauna M. West ◽  
Dominic G. Reeks ◽  
...  
Keyword(s):  
Protein Cleavage ◽  
Site Specific

scholarly journals Functions of KLK4 and MMP-20 in dental enamel formation

2008 ◽  
Vol 389 (6) ◽  
Author(s):  
Yuhe Lu ◽  
Petros Papagerakis ◽  
Yasuo Yamakoshi ◽  
Jan C.-C. Hu ◽  
John D. Bartlett ◽  
...  
Keyword(s):  
Autosomal Recessive ◽  
Dental Enamel ◽  
Organic Matrix ◽  
Maturation Stage ◽  
Protein Cleavage ◽  
Enamel Formation ◽  
Residual Protein ◽  
Kallikrein 4 ◽  
Enamel Protein ◽  
Enamel Proteins

Abstract Two proteases are secreted into the enamel matrix of developing teeth. The early protease is enamelysin (MMP-20). The late protease is kallikrein 4 (KLK4). Mutations in MMP20 and KLK4 both cause autosomal recessive amelogenesis imperfecta, a condition featuring soft, porous enamel containing residual protein. MMP-20 is secreted along with enamel proteins by secretory-stage ameloblasts. Enamel protein-cleavage products accumulate in the space between the crystal ribbons, helping to support them. MMP-20 steadily cleaves accumulated enamel proteins, so their concentration decreases with depth. KLK4 is secreted by transition- and maturation-stage ameloblasts. KLK4 aggressively degrades the retained organic matrix following the termination of enamel protein secretion. The principle functions of MMP-20 and KLK4 in dental enamel formation are to facilitate the orderly replacement of organic matrix with mineral, generating an enamel layer that is harder, less porous, and unstained by retained enamel proteins.

scholarly journals Survival protein anoctamin‐6 controls multiple platelet responses including phospholipid scrambling, swelling, and protein cleavage

2015 ◽  
Vol 30 (2) ◽  
pp. 727-737 ◽  
Author(s):  
Nadine J. A. Mattheij ◽  
Attila Braun ◽  
Roger Kruchten ◽  
Elisabetta Castoldi ◽  
Joachim Pircher ◽  
...  
Keyword(s):  
Protein Cleavage ◽  
Anoctamin 6 ◽  
Phospholipid Scrambling

Secretory Proteases of the Human Skin Microbiome

2021 ◽  
Author(s):  
Wisely Chua ◽  
Si En Poh ◽  
Hao Li
Keyword(s):  
Human Skin ◽  
Hydrolytic Enzymes ◽  
Microbial Interactions ◽  
Skin Microbiome ◽  
Protein Cleavage ◽  
Wide Range ◽  
Range Of Functions ◽  
Diverse Community ◽  
Secreted Proteases ◽  
Pathogenic Agents

The human skin is our outermost layer and serves as a protective barrier against external insults. Advances in next generation sequencing have enabled the discoveries of a rich and diverse community of microbes - bacteria, fungi and viruses that are residents of this surface. The genomes of these microbes also revealed the presence of many secretory enzymes. In particular, proteases which are hydrolytic enzymes capable of protein cleavage and degradation are of special interest in the skin environment which is enriched in proteins and lipids. In this minireview, we will focus on the roles of these skin-relevant microbial secreted proteases, both in terms of their widely studied roles as pathogenic agents in tissue invasion and host immune inactivation, and their recently discovered roles in inter-microbial interactions and modulation of virulence factors. From these studies, it has become apparent that while microbial proteases are capable of a wide range of functions, their expression is tightly regulated and highly responsive to the environments the microbes are in. With the introduction of new biochemical and bioinformatics tools to study protease functions, it will be important to understand the roles played by skin microbial secretory proteases in cutaneous health, especially the less studied commensal microbes with an emphasis on contextual relevance.

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