Results 121 to 130 of about 4,561,775 (254)

Catalytic Properties of ADAM12 and Its Domain Deletion Mutants

open access: yesBiochemistry, 2007
Human ADAM12 (a disintegrin and metalloproteinase) is a multidomain zinc metalloproteinase expressed at high levels during development and in human tumors. ADAM12 exists as two splice variants: a classical type 1 membrane-anchored form (ADAM12-L) and a secreted splice variant (ADAM12-S) consisting of pro, catalytic, disintegrin, cysteine-rich, and EGF ...
Jacobsen, Jonas   +6 more
openaire   +4 more sources

Crystal Structure of the Human Histone Methyltransferase ASH1L Catalytic Domain and Its Implications for the Regulatory Mechanism*

open access: yesJournal of Biological Chemistry, 2011
Absent, small, or homeotic disc1 (Ash1) is a trithorax group histone methyltransferase that is involved in gene activation. Although there are many known histone methyltransferases, their regulatory mechanisms are poorly understood.
S. An, K. Yeo, Y. Jeon, Ji-Joon Song
semanticscholar   +1 more source

Parkin function in Parkinson's disease [PDF]

open access: yes, 2018
Parkinson's disease (PD) is the second most common neurodegenerative disease, and is characterized by involuntary shaking, muscle rigidity, and the progressive loss of dopaminergic neurons.
Arkinson, Connor, Walden, Helen
core   +1 more source

Elucidating the functional significance of catalytic and chitin-binding domains for the anti-cancer property of a bacterial endochitinase

open access: yesJournal of Genetic Engineering and Biotechnology
Chitinases are enzymes that facilitate the breakdown of chitin and also interact with carbohydrate moieties such as heparin sulphate due to structural similarity with chitin, thereby influencing cell adherence and migration.
Ankita Shrivastava   +5 more
doaj   +1 more source

Rational Design of an Orthogonal Pair of Bimolecular RNase P Ribozymes through Heterologous Assembly of Their Modular Domains

open access: yesBiology, 2019
The modular structural domains of multidomain RNA enzymes can often be dissected into separate domain RNAs and their noncovalent assembly can often reconstitute active enzymes.
Yuri Nozawa   +4 more
doaj   +1 more source

Frequent mutation of receptor protein tyrosine phosphatases provides a mechanism for STAT3 hyperactivation in head and neck cancer [PDF]

open access: yes, 2014
The underpinnings of STAT3 hyperphosphorylation resulting in enhanced signaling and cancer progression are incompletely understood. Loss-of-function mutations of enzymes that dephosphorylate STAT3, such as receptor protein tyrosine phosphatases, which ...
Bahar, Ivet   +21 more
core   +1 more source

Rampant exchange of the structure and function of extramembrane domains between membrane and water soluble proteins. [PDF]

open access: yes, 2013
Of the membrane proteins of known structure, we found that a remarkable 67% of the water soluble domains are structurally similar to water soluble proteins of known structure. Moreover, 41% of known water soluble protein structures share a domain with an
Bowie, James U   +3 more
core   +3 more sources

Processing of metacaspase into a cytoplasmic catalytic domain mediating cell death in Leishmania major

open access: yesMolecular Microbiology, 2011
Metacaspases are cysteine peptidases that could play a role similar to caspases in the cell death programme of plants, fungi and protozoa. The human protozoan parasite Leishmania major expresses a single metacaspase (LmjMCA) harbouring a central domain ...
Habib Zalila   +6 more
semanticscholar   +1 more source

Structural and Functional Insights Into Lysostaphin–Substrate Interaction

open access: yesFrontiers in Molecular Biosciences, 2018
Lysostaphin from Staphylococcus simulans and its family enzymes rapidly acquire prominence as the next generation agents in treatment of S. aureus infections.
Helena Tossavainen   +8 more
doaj   +1 more source

Substituting Tyr138 in the active site loop of human phenylalanine hydroxylase affects catalysis and substrate activation

open access: yesFEBS Open Bio, 2017
Mammalian phenylalanine hydroxylase (PAH) is a key enzyme in l‐phenylalanine (l‐Phe) metabolism and is active as a homotetramer. Biochemical and biophysical work has demonstrated that it cycles between two states with a variably low and a high activity ...
João Leandro   +4 more
doaj   +1 more source

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