Results 101 to 110 of about 189,208 (289)

Changes in protein profile during coagulation of latex from Carica papaya

Brazilian Journal of Medical and Biological Research, 1997
We describe the changes in peptide composition by SDS-PAGE analysis of latex from Carica papaya collected at various times after incision of the unripe fruit.
L.G. Silva, O. Garcia, M.T.P. Lopes, C.E. Salas   +3 more
doaj   +1 more source

An inflammatory role for the mammalian carboxypeptidase inhibitor latexin: Relationship to cystatins and the tumor suppressor TIG1 [PDF]

, 2005
Latexin, the only known mammalian carboxypeptidase inhibitor, has no detectable sequence similarity with plant and parasite inhibitors, but it is related to a human putative tumor suppressor protein, TIG1.
Listwan, P., Flanagan, Jack U., Flanagan, JU, Martin, Jennifer L, Listwan, P, Wells, Christine A, Kobe, Bostjan, Hume, DA, Cowieson, Nathan, Martin, Jennifer L., Hume, D A, Ravasi, T., Listwan, Pawel, Kellie, S, Kobe, B., Martin, Jennifer Louise, Cowieson, N. P., Martin, J. L., Huber, T, Huber, Thomas, Aagaard, A, Kobe, B, Flanagan, J. U., Ravasi, Timothy, Aagaard, A., A. Wells, Christine, Wells, C. A., Wells, Christine A., Aagaard, Anna, Wells, Christine, Flanagan, Jack U, Cowieson, N, Kellie, S., Huber, T. L., Hume, David A, Hume, D. A., Kellie, Stuart, Ravasi, T, Hume, David A., Wells, CA, Martin, JL   +40 more
core   +1 more source

Subversion of Atypical Mucin Traps by a Spore‐Coat Effector Blocks Cellular Immunity in Drosophila

Advanced Science, EarlyView.
While the entomopathogenic fungus Metarhizium robertsii can evade insect humoral immunity, its subversion of cellular defenses is still elusive. We identify Eac1 as a spore‐coat protein essential for infecting drosophilids by targeting atypical mucins (Sgf1 and Sgf2), which can entrap spores in a gel matrix and thereby facilitate hemocyte encapsulation.
Shiqin Li, Haimin Chen, Gangqi Fang, Dongxiang Wei, Hongyun Wu, Chen Chen, Song Hong, Chengshu Wang   +7 more
wiley   +1 more source

The cystatins: Protein inhibitors of cysteine proteinases

FEBS Letters, 1991
The last decade has witnessed enormous progress of protein inhibitors of cysteine proteinases concerning their structures, functions and evolutionary relationships. Although they differ in their molecular properties and biological distribution, they are structurally related proteins.
Turk, Vito, Bode, Wolfram
openaire   +2 more sources

A Phosphorylation‐Induced Micellization Switch in the Low‐Complexity Domain of TDP‐43

Advanced Science, EarlyView.
Phosphorylation of TAR DNA‐binding protein's 43 kDa (TDP‐43) low‐complexity domain by casein kinase 1 delta (CK1δ) acts as a molecular switch, redirecting its self‐assembly from macroscopic phase separation toward finite‐sized, spherical block‐copolymer micelles of ∼30 nm.
Rodrigo F. Dillenburg, Anastasia Lopatina, Hao Ruan, Tom Scheidt, Simone Mosna, Emre Pekbilir, Julia Bieber, Frank Schäfer‐Depoix, Katharina Landfester, Carla Schmidt, Martin M. Möckel, Svenja Morsbach, Friederike Schmid, Dorothee Dormann, Lukas Stelzl, Martin Girard, Edward A. Lemke   +16 more
wiley   +1 more source

Expression of schistosomal cathepsin l1 in Escherichia coli and evaluation of its protective capacity in an animal challenge

Journal of Venomous Animals and Toxins including Tropical Diseases, 2009
Schistosomes utilize proteinases to accomplish several activities such as tissue penetration, tissue digestion and evasion of host immune responses.
PA Miyasato, CRR Ramos, PAE Abreu, WO Dias, C Nascimento, PL Ho, T Kawano   +6 more
doaj   +1 more source

A novel cysteine proteinase inhibitor from seeds of Enterolobium contortisiliquum and its effect on Callosobruchus maculatus larvae. [PDF]

Biochem Biophys Rep, 2021
Nunes NNS, Ferreira RS, de Sá LFR, de Oliveira AEA, Oliva MLV.   +4 more
europepmc   +1 more source

The picornaviral 3C proteinases: Cysteine nucleophiles in serine proteinase folds [PDF]

Protein Science, 1995
AbstractThe 3C proteinases are a novel group of cysteine proteinases with a serine proteinase‐like fold that are responsible for the bulk of polyprotein processing in the Picornaviridae. Because members of this viral family are to blame for several ongoing global pandemic problems (rhinovirus, hepatitis A virus) as well as sporadic outbreaks of more ...
openaire   +2 more sources

Purification, refolding and autoactivation of the recombinant cysteine proteinase EhCP112 from Entamoeba histolytica

, 2009
The cysteine proteinase EhCP112 and the adhesin EhADH112 assemble to form the EhCPADH complex involved in Entamoeba histolytica virulence. To further characterize this cysteine proteinase, the recombinant full-length EhCP112 enzyme was expressed and ...
Quintas-Granados, Laura I., Orozco, Esther, Brieba, Luis G., Arroyo, Rossana, Ortega-Lopez, Jaime   +4 more
core   +1 more source

Targeted Degradation of Picornaviral 3C Protease via PROTACs Confers High Barrier to Viral Resistance and Broad‐Spectrum Antiviral Activity

Advanced Science, EarlyView.
This study reports D34 as the first PROTAC degrader that targets the 3C protease of picornaviruses. D34 effectively degrades EV71 3C protease via the ubiquitin‐proteasome pathway. More importantly, D34 exhibits a high resistance barrier and shows broad‐spectrum antiviral activity against multiple picornaviruses, highlighting its potential as a novel ...
Weilong Deng, Junyu Chen, Yingyue Pang, Yuanyuan Zhang, Siqian Chen, Guoliang You, Xiaoman Tian, Zhongxin Xu, Jing Wang, Luqing Shang   +9 more
wiley   +1 more source