Results 181 to 190 of about 771,571 (414)

Protease inhibitors. 2. Bacterial proteases and their inhibitors [PDF]

, 1949
E. S. Duthie, L. Lorenz
openalex   +1 more source

Ionization behavior of the histidine residue in the catalytic triad of serine proteases [PDF]

, 1973
α-Lytic protease is a homologue of the mammalian serine proteases such as trypsin, chymotrypsin, and elastase, and its single histidine residue belongs to the Asp-His-Ser catalytic triad. This single histidine residue has been selectively enriched in the
Hunkapiller, Michael W., Richards, John H., Smallcombe, Stephen H., Whitaker, Don R.   +3 more
core  

Ubiquitination of transcription factors in cancer: unveiling therapeutic potential

Molecular Oncology, EarlyView.
In cancer, dysregulated ubiquitination of transcription factors contributes to the uncontrolled growth and survival characteristics of tumors. Tumor suppressors are degraded by aberrant ubiquitination, or oncogenic transcription factors gain stability through ubiquitination, thereby promoting tumorigenesis.
Dongha Kim, Hye Jin Nam, Sung Hee Baek
wiley   +1 more source

Serum Anti-Proteases in the Leukemias [PDF]

, 1951
Philip M. West, BETTY W. SMITH
openalex   +1 more source

Aberrant expression of nuclear prothymosin α contributes to epithelial‐mesenchymal transition in lung cancer

Molecular Oncology, EarlyView.
Nuclear prothymosin α inhibits epithelial‐mesenchymal transition (EMT) in lung cancer by increasing Smad7 acetylation and competing with Smad2 for binding to SNAI1, TWIST1, and ZEB1 promoters. In early‐stage cancer, ProT suppresses TGF‐β‐induced EMT, while its loss in the nucleus in late‐stage cancer leads to enhanced EMT and poor prognosis.
Liyun Chen, Chung‐Teng Wang, Jia‐Ming Chang, Ai‐Li Shiau, Gia‐Shing Shieh, Yau‐Lin Tseng, Yi‐Ting Yen, Tang‐Hsiu Huang, Li‐Hsin Cheng, Yu‐Chih Wu, Chao‐Liang Wu, Bing‐Hua Su, Pensee Wu   +12 more
wiley   +1 more source

Involvement of a Complement-Like Factor in the Activation of Blood Protease [PDF]

, 1952
Walton B. Geiger
openalex   +1 more source

Determination of ADP/ATP translocase isoform ratios in malignancy and cellular senescence

Molecular Oncology, EarlyView.
The individual functions of three isoforms exchanging ADP and ATP (ADP/ATP translocases; ANTs) on the mitochondrial membrane remain unclear. We developed a method for quantitatively differentiating highly similar human ANT1, ANT2, and ANT3 using parallel reaction monitoring. This method allowed us to assess changes in translocase levels during cellular
Zuzana Liblova, Dominika Maurencova, Barbora Salovska, Marek Kratky, Tomas Mracek, Zuzana Korandova, Alena Pecinova, Pavla Vasicova, David Rysanek, Ladislav Andera, Ivo Fabrik, Rudolf Kupcik, Pavel Kashmel, Pinky Sultana, Vojtech Tambor, Jiri Bartek, Josef Novak, Marie Vajrychova, Zdenek Hodny   +18 more
wiley   +1 more source

Molecular Dynamics Studies on HIV-1 Protease: Drug Resistance and Folding Pathways [PDF]

arXiv, 2001
Drug resistance to HIV-1 Protease involves accumulation of multiple mutations in the protein. Here we investigate the role of these mutations by using molecular dynamics simulations which exploit the influence of the native-state topology in the folding process.
arxiv  

Mapping Hsp104 interactions using cross‐linking mass spectrometry

FEBS Open Bio, EarlyView.
This study examines how cross‐linking mass spectrometry can be utilized to analyze ATP‐induced conformational changes in Hsp104 and its interactions with substrates. We developed an analytical pipeline to distinguish between intra‐ and inter‐subunit contacts within the hexameric homo‐oligomer and discovered contacts between Hsp104 and a selected ...
Kinga Westphal, Karolina Michalska, Andrzej Joachimiak, Lukasz A. Joachimiak   +3 more
wiley   +1 more source

Crucial stages of protein folding through a solvable model: predicting target sites for enzyme-inhibiting drugs [PDF]

Protein Science, Vol.11, p. 1878-1887 (2002), 2002
An exactly solvable model based on the topology of a protein native state is applied to identify bottlenecks and key-sites for the folding of HIV-1 Protease. The predicted sites are found to correlate well with clinical data on resistance to FDA-approved drugs.
arxiv