About: PKCS is a research topic. Over the lifetime, 124 publications have been published within this topic receiving 5223 citations. The topic is also known as: PKCS.
TL;DR: This memo represents a republication of PKCS #1 v2.1 from RSA Laboratories' Public-Key Cryptography Standards (PKCS) series, and change control is retained within the PKCS process.
Abstract: This memo represents a republication of PKCS #1 v2.1 from RSA Laboratories' Public-Key Cryptography Standards (PKCS) series, and change control is retained within the PKCS process. The body of this document is taken directly from the PKCS #1 v2.1 document, with certain corrections made during the publication process.
TL;DR: The protein kinase C (PKC) family consists of 11 isoenzymes that, due to structural and enzymatic differences, can be subdivided into three groups: the Ca2+-dependent, diacylglycerol (DAG)-activated cPKCs (conventional PKCs: α, β1, β2, γ); the Ca 2+-independent, DAG-activated nPKC (novel PKC: δ, e, η, θ, μ).
Abstract: The protein kinase C (PKC) family consists of 11 isoenzymes that, due to structural and enzymatic differences, can be subdivided into three groups: The Ca2+-dependent, diacylglycerol (DAG)-activated cPKCs (conventional PKCs: α, β1, β2, γ); the Ca2+-independent, DAG-activated nPKCs (novel PKCs: δ, e, η, θ, μ), and the Ca2+-dependent, DAG non-responsive aPKCs (atypical PKCs: ζ, λ/ι). PKCμ is a novel PKC, but with some special structural and enzymatic properties.
TL;DR: In this paper, the authors recognized that C2 domains are also present in Ca(2+)-independent protein kinases (delta, epsilon, eta, and theta), other kinases, a eukaryotic PLD, the breakpoint cluster region (BCR) gene product, and two further GAPs.
Abstract: Various membrane lipid metabolites, generated by phospholipases C and D (PLCs, PLDs), are known to regulate the activities of protein kinases C (PKCs) and GTP-ase activating proteins (GAPs) in a range of cellular processes. Conventional Ca(2+)-dependent PKCs (alpha, beta I, beta II, and gamma), PLCs and various GAPs are all known to contain copies of a phospholipid-binding domain, termed C2 or CalB. Here we recognize that C2 domains are also present in "new" Ca(2+)-independent PKCs (delta, epsilon, eta, and theta), other kinases, a eukaryotic PLD, the breakpoint cluster region (BCR) gene product, and two further GAPS. Twenty-two previously unrecognized C2 domain sequences are presented, which include a single copy in the mammalian poreforming proteins, perforin.
TL;DR: This document represents a republication of PKCS #12 v1.1 from RSA Laboratories' Public Key Cryptography Standard (PKCS) series and change control is transferred to the IETF.
Abstract: PKCS #12 v1.1 describes a transfer syntax for personal identity
information, including private keys, certificates, miscellaneous
secrets, and extensions. Machines, applications, browsers, Internet
kiosks, and so on, that support this standard will allow a user to
import, export, and exercise a single set of personal identity
information. This standard supports direct transfer of personal
information under several privacy and integrity modes. This document
represents a republication of PKCS #12 v1.1 from RSA Laboratories'
Public Key Cryptography Standard (PKCS) series. By publishing this
RFC, change control is transferred to the IETF.
TL;DR: The involvement of PKCs in health and disease and the importance of redox signaling in the regulation of this family of kinases are summarized.
Abstract: Hormones, growth factors, electrical stimulation, and cell–cell interactions regulate numerous cellular processes by altering the levels of second messengers, thus influencing biochemical reactions inside the cells. The Protein Kinase C family (PKCs) is a group of serine/threonine kinases that are dependent on calcium (Ca2+), diacylglycerol, and phospholipids. Signaling pathways that induce variations on the levels of PKC activators have been implicated in the regulation of diverse cellular functions and, in turn, PKCs are key regulators of a plethora of cellular processes, including proliferation, differentiation, and tumorigenesis. Importantly, PKCs contain regions, both in the N-terminal regulatory domain and in the C-terminal catalytic domain, that are susceptible to redox modifications. In several pathophysiological conditions when the balance between oxidants, antioxidants, and alkylants is compromised, cells undergo redox stress. PKCs are cell-signaling proteins that are particularly sensi...