Russell McCandliss

Bio: Russell McCandliss is an academic researcher from Roche Institute of Molecular Biology. The author has contributed to research in topics: IRF8 & Interleukin 29. The author has an hindex of 3, co-authored 3 publications receiving 536 citations.

The structure of eight distinct cloned human leukocyte interferon cDNAs.

Abstract: Eight classes of human leukocyte interferon (LeIFN) cDNA clones have been identified in a cDNA library prepared from a myeloblastoid cell line. The nucleotide sequences demonstrate that the multiple human LeIFN genes code for a family of homologous, yet distinct proteins. One of the cDNA clones may have been derived from the transcription of a LeIFN pseudogene.

Patterns of Amino Acids near Signal‐Sequence Cleavage Sites

Abstract: According to the signal hypothesis, a signal sequence, once having initiated export of a growing protein chain across the rough endoplasmic reticulum, is cleaved from the mature protein at a specific site. It has long been known that some part of the cleavage specificity resides in the last residue of the signal sequence, which invariably is one with a small, uncharged side-chain, but no further specific patterns of amino acids near the point of cleavage have been discovered so far. In this paper, some such patterns, based on a sample of 78 eukaryotic signal sequences, are presented and discussed, and a first attempt at formulating rules for the prediction of cleavage sites is made.

Interferons at age 50: past, current and future impact on biomedicine.

Abstract: The family of interferon (IFN) proteins has now more than reached the potential envisioned by early discovering virologists: IFNs are not only antivirals with a spectrum of clinical effectiveness against both RNA and DNA viruses, but are also the prototypic biological response modifiers for oncology, and show effectiveness in suppressing manifestations of multiple sclerosis. Studies of IFNs have resulted in fundamental insights into cellular signalling mechanisms, gene transcription and innate and acquired immunity. Further elucidation of the multitude of IFN-induced genes, as well as drug development strategies targeting IFN production via the activation of the Toll-like receptors (TLRs), will almost certainly lead to newer and more efficacious therapeutics. Our goal is to offer a molecular and clinical perspective that will enable IFNs or their TLR agonist inducers to reach their full clinical potential.

Existence of distinct sodium channel messenger RNAs in rat brain

Abstract: The sodium channel is a voltage-gated ionic channel essential for the generation of action potentials1–3. It has been reported that the sodium channels purified from the electric organ of Electrophorus electricus (electric eel)4,5 and from chick cardiac muscle6 consist of a single polypeptide of relative molecular mass (Mr) ∼260,000 (260K), whereas those purified from rat brain7 and skeletal muscle8 contain, in addition to the large polypeptide, two or three smaller polypeptides of Mr 37–45K. Recently, we have elucidated the primary structure of the Electrophorus sodium channel by cloning and sequencing the DNA complementary to its messenger RNA9. Despite the apparent homogeneity of the purified sodium channel preparations, several types of tetrodotoxin (or saxitoxin) binding sites or sodium currents have been observed in many excitable membranes10–19. The occurrence of distinguishable populations of sodium channels may be attributable to different states of the same channel protein or to distinct channel proteins. We have now isolated complementary DNA clones derived from two distinct rat brain mRNAs encoding sodium channel large polypeptides and present here the complete amino-acid sequences of the two polypeptides (designated sodium channels I and II), as deduced from the cDNA sequences. A partial DNA sequence complementary to a third homologous mRNA from rat brain has also been cloned.