Results 41 to 50 of about 776,967 (309)

The Serine Recombinases

open access: yesMicrobiology Spectrum, 2014
ABSTRACTIn site-specific recombination, two short DNA sequences (‘sites’) are each cut at specific points in both strands, and the cut ends are rejoined to new partners. The enzymes that mediate recognition of the sites and the subsequent cutting and rejoining steps are called recombinases.
openaire   +2 more sources

Capitao_supplementary_information – Supplemental material for A single administration of ‘microbial’ D-alanine to healthy volunteers augments reaction to negative emotions: A comparison with D-serine

open access: yes, 2020
Supplemental material, Capitao_supplementary_information for A single administration of ‘microbial’ D-alanine to healthy volunteers augments reaction to negative emotions: A comparison with D-serine by Liliana P Capitão, Jessica Forsyth, Mia A Thomaidou,
Mark D Condon (8577036)   +5 more
core   +1 more source

Primary structure of potato Kunitz-type serine proteinase inhibitor [PDF]

open access: yes, 2000
The serine proteinase inhibitor (PSPI-51) isolated from potato tubers (Solanum tuberosum L,) comprises two protein species with pi 5.2 and 6.3, denoted as PSPI-21-5.2 and PSPI-21-6.3, respectively.
Mentele, Reinhard   +3 more
core   +1 more source

Degradation mechanism of the von Willebrand factor A2 domain by nattokinase

open access: yesFEBS Letters, EarlyView.
Nattokinase, a natto‐derived protease, exhibits potent antithrombotic effects. This study demonstrates that nattokinase directly cleaves the von Willebrand factor (vWF) A2 domain in vitro. Unlike the native regulator ADAMTS13, nattokinase degrades folded vWF independently of shear stress.
Ryuichi Hyakumoto   +3 more
wiley   +1 more source

A Short and Efficient Synthesis of l-5,5,5,5‘,5‘,5‘-hexafluoroleucine from N-Cbz-l-Serine

open access: yes, 2016
5,5,5,5‘,5‘,5‘-Hexafluoroleucine (6), a fluorous analogue of leucine, is of considerable interest as a building block in the design of fluorous proteins and peptides.
James T. Anderson (218373)   +2 more
core   +1 more source

Amperometric Self-Referencing Ceramic Based Microelectrode Arrays for D-Serine Detection [PDF]

open access: yes, 2018
D-serine is the major D-amino acid in the mammalian central nervous system. As the dominant co-agonist of the endogenous synaptic NMDA receptor, D-serine plays a role in synaptic plasticity, learning, and memory.
Campos-Beltran, Diana   +16 more
core   +1 more source

ABL kinase‐dependent phosphorylation of SH proteins promotes their direct interaction with CRK family SH2 domains

open access: yesFEBS Letters, EarlyView.
CT10 regulator of kinase (CRK) and CRK‐Like (CRKL) are signaling adaptors driving cell adhesion, motility, differentiation, and proliferation. SH2‐domain containing (SH) proteins are enriched in YXXP motifs which when phosphorylated create preferred binding sites for CRK family SH2 domains.
Phoebe M. Cousens   +8 more
wiley   +1 more source

Engineering peptides into antibodies—opportunities and strategies for therapeutic innovation

open access: yesFEBS Letters, EarlyView.
Peptides and antibodies occupy complementary therapeutic niches. Peptides recognize difficult targets in a compact format, while antibodies add specificity, long half‐life, and effector functions. This review examines strategies that merge both modalities—peptide grafting into loops, terminal and Fc fusions, and bioconjugation—highlighting how ...
Jinling Wang   +2 more
wiley   +1 more source

D-Serine and Serine Racemase

open access: yesHans Journal of Biomedicine, 2013
D-丝氨酸主要存在于哺乳动物的前脑,海马区和纹状体,作为胶质细胞释放的神经递质,作用于NMDA (N-methyl-D-aspartate receptor)受体,引起中枢神经系统中信号的传导。在突触可塑性,学习和记忆等方面起重要作用。丝氨酸消旋酶是一种磷酸吡多醛依赖酶,在ATP和Mg2+的辅助下,通过消旋作用将L型丝氨酸转变为D型丝氨酸。对于神经及精神性疾病,丝氨酸消旋酶可能是一个新的治疗靶点。本文从D-丝氨酸和丝氨酸消旋酶的结构性质,作用机理,功能,调控等方面进行了阐述。 D-serine mainly distributed in the mammalian forebrain, hippocampus and striatum, which as neurotransmit-ters ...
openaire   +1 more source

PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163

open access: yesFEBS Letters, 1996
The 80kDa yristolated lanine‐ich ‐inase ubstrate (MARCKS) in a major in vivo substrate of protein kinase C (PKC). Here we report that MARCKS is a major substrate for the lipid‐activated PKC‐related kinase (PRK1) in cell extracts. Furthermore, PRK1 is shown to phosphorylate MARCKS on the same sites as PKC in vitro.
Palmer, Ruth H.   +5 more
openaire   +2 more sources

Home - About - Disclaimer - Privacy