Gregory M. Lipkind

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A computer-assisted structural analysis of regular polysaccharides on the basis of 13C-n.m.r. data.

Gregory M. Lipkind, Aleksander S Shashkov, Yuriy A. Knirel, Evgeny V Vinogradov, Nikolay K. Kochetkov
Carbohydrate research
1988

A computerised approach to the structural analysis of unbranched regular polysaccharides is described, which is based on an evaluation of the 13C-n.m.r. spectra for all possible primary structures… (More)

Insulin gene mutations as a cause of permanent neonatal diabetes.

Julie Støy, Emma L. Edghill, +15 authors Graeme I. Bell
Proceedings of the National Academy of Sciences…
2007

We report 10 heterozygous mutations in the human insulin gene in 16 probands with neonatal diabetes. A combination of linkage and a candidate gene approach in a family with four diabetic members led… (More)

KcsA crystal structure as framework for a molecular model of the Na(+) channel pore.

The crystal structure of the pore-forming part of the KcsA bacterial K(+)-selective channel suggests a possible motif for related voltage-gated channels. We examined the hypothesis that the spacial… (More)

Proteolytic Processing Mechanisms in the Biosynthesis of Neuroendocrine Peptides: The Subtilisin-like Proprotein Convertases

Yves Rouillé, Stephen J. Duguay, +6 authors Donald F. Steiner
Frontiers in Neuroendocrinology
1995

The recent discovery of a novel family of precursor processing endoproteases has greatly accelerated progress in understanding the complex mechanisms underlying the maturation of prohormones,… (More)

Identification of 14 new glucokinase mutations and description of the clinical profile of 42 MODY-2 families

Gilberto Velho, Hélène Blanché, +12 authors Philippe Froguel
Diabetologia
1997

Mutations in glucokinase are associated with defects in insulin secretion and hepatic glycogen synthesis resulting in mild chronic hyperglycaemia, impaired glucose tolerance or diabetes mellitus. We… (More)

A structural model of the tetrodotoxin and saxitoxin binding site of the Na+ channel.

Gregory M. Lipkind, Harry A. Fozzard
Biophysical journal
1994

Biophysical evidence has placed the binding site for the naturally occurring marine toxins tetrodotoxin (TTX) and saxitoxin (STX) in the external mouth of the Na+ channel ion permeation pathway. We… (More)

Molecular modeling of local anesthetic drug binding by voltage-gated sodium channels.

Gregory M. Lipkind, Harry A. Fozzard
Molecular pharmacology
2005

Voltage-gated sodium (Na+) channels are targets for local anesthetic (LA) drugs that bind in the inner pore of the channel with affinities related to the channel gating states. Our core model of the… (More)

Inhibition of furin by polyarginine-containing peptides: nanomolar inhibition by nona-D-arginine.

Magdalena M Kacprzak, Juan Ramón Peinado, +6 authors Iris Lindberg
The Journal of biological chemistry
2004

Polyarginine-containing peptides represent potent inhibitors of furin, a mammalian endoprotease that plays an important role in metabolism, activation of pathogenic toxins, and viral proliferation.… (More)

Differences in saxitoxin and tetrodotoxin binding revealed by mutagenesis of the Na+ channel outer vestibule.

J L Penzotti, Harry A. Fozzard, Gregory M. Lipkind, Samuel C Dudley
Biophysical journal
1998

The marine guanidinium toxins, saxitoxin (STX) and tetrodotoxin (TTX), have played crucial roles in the study of voltage-gated Na+ channels. Because they have similar actions, sizes, and functional… (More)

Predominant interactions between mu-conotoxin Arg-13 and the skeletal muscle Na+ channel localized by mutant cycle analysis.

Nam Soo Chang, Robert J. French, Gregory M. Lipkind, Harry A. Fozzard, Samuel C Dudley
Biochemistry
1998

High-affinity mu-conotoxin block of skeletal muscle Na+ channels depends on an arginine at position 13 (Arg-13). To understand both the mechanism of toxin interaction and the general structure of its… (More)

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