Results 331 to 340 of about 128,354 (367)

Purification and identification of a novel and four known serine proteinase inhibitors secreted by human glioblastoma cells.

Journal of Biochemistry (Tokyo), 1996
Our previous studies have shown that some human cancer cell lines produce pancreatic trypsinogen, plasminogen, and tissue-type kallikrein. To understand the regulatory mechanism of these proteinases, serine proteinase inhibitors secreted by human ...
N. Koshikawa, Takashi Nakamura, Naoto Tsuchiya, Mitsuko Isaji, H. Yasumitsu, Makoto Umeda, Kaoru Miyazaki   +6 more
semanticscholar   +1 more source

An evolutionarily conserved binding site for serine proteinase inhibitors in large conductance calcium-activated potassium channels.

Biochemistry, 1996
Complementary DNA coding for the channel-forming alpha-subunit of a large conductance Ca(2+)-activated K+ channel (maxi Kca channel) was cloned from bovine aortic smooth muscle cells.
G. Moss, J. Marshall, M. Morabito, J. Howe, E. Moczydlowski   +4 more
semanticscholar   +1 more source

Cationic Inhibitors of Serine Proteinases from Buckwheat Seeds

Biochemistry (Moscow), 2001
Preparations of low molecular weight protein inhibitors of serine proteinases have been obtained from buckwheat (Fagopyrum esculentum) seeds by chromatography of seed extract on trypsin-Sepharose 4B, Mono-Q, and Mono-S ion exchangers (FPLC regime). Their molecular masses, determined by mass spectrometry, were 5203 (BWI-1c), 5347 (BWI-2c), 7760 (BWI-3c),
Yakov E. Dunaevsky, A. Kh. Musolyamov, T. A. Tsybina, Tsezi A. Egorov, Mikhail A. Belozersky   +4 more
openaire   +3 more sources

The complete amino acid sequences of two serine proteinase inhibitors from the fruiting bodies of a basidiomycete, Pleurotus ostreatus.

Archives of Biochemistry and Biophysics, 1995
The complete amino acid sequences of two isomeric endogenous inhibitors, IA-1 and IA-2, both of which specifically inhibit an intracellular serine proteinase (proteinase A) purified from the fruiting bodies of a higher basidiomycete, Pleurotus ostreatus,
N. Dohmae, K. Takio, Y. Tsumuraya, Y. Hashimoto   +3 more
semanticscholar   +1 more source

Inhibitor Complexes of the Pseudomonas Serine-Carboxyl Proteinase

Biochemistry, 2001
Crystal structures of the serine-carboxyl proteinase from Pseudomonas sp. 101 (PSCP), complexed with a number of inhibitors, have been solved and refined at high- to atomic-level resolution. All of these inhibitors (tyrostatin, pseudo-tyrostatin, AcIPF, AcIAF, and chymostatin, as well as previously studied iodotyrostatin and pseudo-iodotyrostatin) make
Kohei Oda, Mi Li, Zbigniew Dauter, Alexander Wlodawer, Ben M. Dunn, Alla Gustchina, Hiroshi Oyama, Nathan E. Goldfarb, Kenichi Uchida   +8 more
openaire   +3 more sources

LEKTI: a multidomain serine proteinase inhibitor with pathophysiological relevance

The International Journal of Biochemistry & Cell Biology, 2002
Proteinase inhibitors are important negative regulators of proteinase action in vivo and are thus involved in several pathophysiological processes. Starting with the isolation of two new peptides from human blood filtrate, we succeeded in cloning a cDNA encoding the precursor protein for a novel 15-domain Kazal-type-related serine proteinase inhibitor.
Hans-Jürgen Mägert, Katrin Drogemuller, Michael Walden, Peter Kreutzmann, Wolf-Georg Forssmann, Ludger Ständker   +5 more
openaire   +3 more sources

Peptidic Inhibitors of Serine Proteinases of Plant Origin

2013
Serine proteinases play important roles in many physiological processes and in consequence, when unbalanced, are responsible for numerous severe diseases. The most predominant mechanism of their control is the ubiquitous presence of their inhibitors.
Anna Łęgowska, Adam Lesner, Krzysztof Rolka, Magdalena Wysocka   +3 more
openaire   +2 more sources

The Role of Scaffolding in Standard Mechanism Serine Proteinase Inhibitors

Protein & Peptide Letters, 2005
In single domain, "standard mechanism" protein inhibitors of serine proteinases, about a dozen residues make contact with the cognate enzyme. The remainder of the molecule, the scaffolding, holds the reactive site region of the inhibitor in a canonical conformation, improves the binding by about six orders of magnitude and protects it from proteolysis.
Clyde A. Kelly, M. A. Qasim, Michael Laskowski   +2 more
openaire   +3 more sources

Partial characterization of novel serine proteinase inhibitors from human umbilical vein endothelial cells.

Archives of Biochemistry and Biophysics, 1995
Serine proteinase inhibitors play major roles in physiological and pathophysiological processes such as angiogenesis, intravascular fibrinolysis, wound healing, and tumor invasion, and metastasis.
C. N. Rao, D. Gomez, D. Woodley, U. Thorgeirsson   +3 more
semanticscholar   +1 more source

Gene regulation of the serine proteinase inhibitors α1-antitrypsin and α1-antichymotrypsin

, 2001
The serine proteinase inhibitors (serpins) are a superfamily of proteins with a diverse set of functions, including the control of blood coagulation, complement activation, programmed cell death and development.
N. Kalsheker, S. Morley, K. Morgan
semanticscholar   +1 more source