Results 131 to 140 of about 3,702 (189)

Identification of maternal antibodies targeting a cystatin-like protein of Trichinella spiralis in offspring. [PDF]

Parasites Hosts Dis
Cho M, Yu HS.
europepmc   +1 more source

DNA Modulates Structural Transitions and Oligomerization Kinetics of the Functional Amyloid CRES. [PDF]

J Am Chem Soc
Kukreja R, Canny MD, Cornwall GA, Latham MP.   +3 more
europepmc   +1 more source

Comparative Proteomic Analysis of Self-Compatible <i>Turnera</i> Mutants Suggests <i>Glutathione S-Transferase 8</i> Is Involved in Overcoming S-Morph Female Self-Incompatibility Response. [PDF]

Plant Direct
Henning PM, Chafe PDJ, Hamam HJ, Shore JS.   +3 more
europepmc   +1 more source

Acquired pellicle engineering: a fascinating approach to prevent demineralization. [PDF]

J Appl Oral Sci
Ferrari CR, Hannig M, Buzalaf MAR.
europepmc   +1 more source

Assessing diagnostic, vaccine and therapeutic potential of selected <i>Trichinella</i> proteins. [PDF]

Food Waterborne Parasitol
Stachyra A, Bień-Kalinowska J.
europepmc   +1 more source

Identification of the protease inhibitory domain of Trichinella spiralis novel cystatin (TsCstN). [PDF]

Parasites Hosts Dis
Yuthithum T, Phuphisut O, Reamtong O, Kosoltanapiwat N, Chaimon S, Kobpornchai P, Thawornkuno C, Malaithong P, Sawatdichaikul O, Adisakwattana P.   +9 more
europepmc   +1 more source

Time- and Genotype-Dependent Root-Transcriptomic Responses of Soybean to Combined Soybean Aphid and Soybean Cyst Nematode Infestation. [PDF]

Plants (Basel)
Neupane S, Varenhorst AJ, Nepal MP.
europepmc   +1 more source

Investigation of CST7 and hsa-miR-4793-5p gene expression in breast cancer. [PDF]

Biochem Biophys Rep
Kalaki NS, Ahmadzadeh M, Dehghan M, Shahabi Rabori V, Davoudi S, Afkhami H.   +5 more
europepmc   +1 more source

Update on the Physiopathology of Keratoconus. [PDF]

Med Sci (Basel)
Barcelo-Canton RH, Rodriguez-Garcia A, Graue-Hernandez EO, Mehta JS.   +3 more
europepmc   +1 more source

Immunomodulatory properties of cystatins

Cellular and Molecular Life Sciences, 2002
Cystatins are natural tight-binding reversible inhibitors of cysteine proteases. Because these cysteine proteases exist in all living organisms and because they are involved in various biological and pathological processes, the control of these protease ...
Susanne Hartmann, B Vray
exaly   +5 more sources