The recognition of ubiquitylated substrates is an essential element of ubiqu-itin⁄26S proteasome-mediated proteolysis (UPP), which is mediated directly
by the proteasome subunit RPN10 and⁄or RPN13, or indirectly by ubiquitin
receptors containing ubiquitin-like and ubiquitin-associated domains. By
pull-down and mutagenesis assays, we detected cross-species divergence of
the major recognition pathways.
Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: Characterization of vaccinia virus A12L protein proteolysis and its participation in virus assembly
Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài:
Vaccinia virus A12L protein and its AG/A proteolysis play an important role in viral morphogenic transition
Tham khảo tài liệu 'báo cáo hóa học: " vaccinia virus a12l protein and its ag/a proteolysis play an important role in viral morphogenic transition"', luận văn - báo cáo phục vụ nhu cầu học tập, nghiên cứu và làm việc hiệu quả
Tham khảo tài liệu 'báo cáo hóa học: " characterization of vaccinia virus a12l protein proteolysis and its participation in virus assembly"', luận văn - báo cáo phục vụ nhu cầu học tập, nghiên cứu và làm việc hiệu quả
Lactoferrin (LF) is an iron-binding glycoprotein of the
innate host defence system. To elucidate the role ofN-linked
glycosylation in protection of LF against proteolysis, we
compared the tryptic susceptibility of human LF (hLF)
variants from human milk, expressed in human 293(S) cells
or in the milk of transgenic mice and cows. The analysis
revealed that recombinant hLF (rhLF) with mutations
Ile130fiThr and Gly404fiCys was about twofold more
susceptible than glycosylated and unglycosylated variants
with the naturally occurring Ile130 and Gly404....
Breast cancer cells exhibit excessive proteolysis, which is responsible for
extensive extracellular matrix degradation, invasion and metastasis. Besides
other proteases, lysosomal cysteine protease cathepsin B has been impli-cated in these processes and the impairment of its intracellular activity was
suggested to reduce harmful proteolysis and hence diminish progression of
A detailed proteolysis study of internalized diphtheria toxin (DT) within
rat liver endosomes was undertaken to determine whether DT-resistant
species exhibit defects in toxin endocytosis, toxin activation by cellular
enzymes or toxin translocation to its cytosolic target.
Limited proteolysis in combination with liquid chromatography-ion trap
mass spectrometry (LC-MS) was used to analyze engineered or natural
proteins derived from a type I modular polyketide synthase (PKS), the
6-deoxyerythronolide B synthase (DEBS), and comprising either the first
two extension modules linked to the chain-terminating thioesterase (TE)
(DEBS1-TE); or the last two extension modules (DEBS3) or the first exten-sion module linked to TE (diketide synthase, DKS).
Cytidine 5¢-triphosphate synthase catalyses the ATP-dependent formation of CTP from UTP using either
ammonia orL-glutamine as the source of nitrogen. When
glutamine is the substrate, GTP is required as an allosteric
effector to promote catalysis. Limited trypsin-catalysed
proteolysis, Edman degradation, and site-directed muta-genesis were used to identify peptide bonds C-terminal to
three basic residues (Lys187, Arg429, and Lys432) of
Escherichia coliCTP synthase thatwere highly susceptible to
Bovineb-lactoglobulin was hydrolyzed with trypsin or
chymotrypsin in the course of heat treatment at 55, 60 and
65°C at neutral pH. At these temperaturesb-lactoglobulin
undergoes signi®cant but reversible structural changes. In
the conditions used in the present study,b-lactoglobulinwas
virtually insensitive to proteolysis by either enzyme at room
temperature, but underwent extensive proteolysis when
either proteasewas present during the heat treatment.
Vibrio mimicusis a causative agent of human gastroenteritis and food
poisoning, and this species produces an enterotoxic hemolysin (V. mimi-cus hemolysin) as a virulence determinant. Vibrio mimicushemolysin is
secreted as an 80 kDa precursor, which is later converted to the 66 kDa
mature toxin through removal of an N-terminal propeptide via cleavage
of the Arg151–Ser152 bond.
Trappin-2 (also known as pre-elafin) is an endogenous inhibitor of neutro-phil serine proteases and is involved in the control of excess proteolysis,
especially in inflammatory events, along with the structurally related secre-tory leucocyte proteinase inhibitor.
Bacillus cereusis an opportunistic pathogenic bacterium closely related to
Bacillus anthracis, the causative agent of anthrax in mammals. A significant
portion of theB. cereuschromosomal genes are common to B. anthracis,
including genes which in B. anthraciscode for putative virulence and sur-face proteins.
Snake venom metalloproteinases (SVMPs) have recently been shown to
interact with proteins containing von Willebrand factor A (VWA) domains,
including the extracellular matrix proteins collagen XII, collagen XIV, mat-rilins 1, 3 and 4, and von Willebrand factor (VWF) via their cysteine-rich
A 37 residue peptide, aglycin, has been purified from porcine intestine. The
sequence is identical to that of residues 27–63 of plant albumin 1 B precur-sor (PA1B, chain b) from pea seeds. Aglycin resists in vitro proteolysis by
pepsin, trypsin and Glu-C protease, compatible with its intestinal occur-rence and an exogenous origin from plant food.
The CIII protein of bacteriophage lambda exhibits antiproteolytic activity
against the ubiquitous metalloprotease HflB (FtsH) of Escherichia coli,
thereby stabilizing the kCII protein and promoting lysogenic development
of the phage. CIII also protectsE. colir
, another substrate of HflB.
Calpains are intracellular Ca
-regulated cysteine pro-teases which mediate regulatory cleavage of specific
substrates. They cover a broad range of physiological
functions including proteolysis of molecules involved
in cytoskeletal organization, the cell cycle, signal trans-duction, apoptosis, and protein renewal during growth
and tissue regeneration. Originally found in mamma-lian skeletal muscle then in numerous organisms inclu-ding protists and plants, their expression is ubiquitous