Results 121 to 130 of about 793,529 (384)

Tonic signaling of the B‐cell antigen‐specific receptor is a common functional hallmark in chronic lymphocytic leukemia cell phosphoproteomes at early disease stages

open access: yesMolecular Oncology, EarlyView.
B‐cell chronic lymphocytic leukemia (B‐CLL) and monoclonal B‐cell lymphocytosis (MBL) show altered proteomes and phosphoproteomes, analyzed using mass spectrometry, protein microarrays, and western blotting. Identifying 2970 proteins and 316 phosphoproteins, including 55 novel phosphopeptides, we reveal BCR and NF‐kβ/STAT3 signaling in disease ...
Paula Díez   +17 more
wiley   +1 more source

Serine Proteases of Parasitic Helminths

open access: yesKorean Journal of Parasitology, 2015
Serine proteases form one of the most important families of enzymes and perform significant functions in a broad range of biological processes, such as intra- and extracellular protein metabolism, digestion, blood coagulation, regulation of development ...
Yong Yang   +6 more
semanticscholar   +1 more source

Components of cell-matrix linkage as potential new markers for prostate cancer [PDF]

open access: yes, 2011
Prostate cancer is one of the most common tumor diseases worldwide. Often being non-aggressive, prostate tumors in these cases do not need immediate treatment.
Eble, Johannes Andreas, Navdaev, Alexey
core   +2 more sources

Ubiquitination of transcription factors in cancer: unveiling therapeutic potential

open access: yesMolecular 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

The protease inhibitors

open access: yesPrimary Care Update for OB/GYNS, 2001
With the advent of newer antiretroviral agents for the treatment of patients with human immunodeficiency virus (HIV) infection and acquired immune deficiency syndrome (AIDS), health care providers are faced with many options to optimize their patients' therapy.
College of Medicine, University of Florida, Gainesville, Florida, USA ( host institution )   +1 more
openaire   +4 more sources

Activity-based profiling of proteases.

open access: yesAnnual Review of Biochemistry, 2014
Proteolytic enzymes are key signaling molecules in both normal physiological processes and various diseases. After synthesis, protease activity is tightly controlled.
L. Sanman, M. Bogyo
semanticscholar   +1 more source

Digestion of Protein in Premature and Term Infants. [PDF]

open access: yes, 2012
Premature birth rates and premature infant morbidity remain discouragingly high. Improving nourishment for these infants is the key for accelerating their development and decreasing disease risk. Dietary protein is essential for growth and development of
Dallas, David C   +3 more
core   +2 more sources

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

open access: yesMolecular 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   +12 more
wiley   +1 more source

IgA1 protease

open access: yesThe International Journal of Biochemistry & Cell Biology, 2006
IgA1 proteases are proteolytic enzymes that cleave specific peptide bonds in the human immunoglobulin A1 (IgA1) hinge region sequence. Several species of pathogenic bacteria secrete IgA1 proteases at mucosal sites of infection to destroy the structure and function of human IgA1 thereby eliminating an important aspect of host defence. IgA1 proteases are
Mistry, Dippica, Stockley, Robert A.
openaire   +2 more sources

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

open access: yes, 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.   +3 more
core  

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